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. 1989 Dec;53(4):450–490. doi: 10.1128/mr.53.4.450-490.1989

Protein phosphorylation and regulation of adaptive responses in bacteria.

J B Stock, A J Ninfa, A M Stock
PMCID: PMC372749  PMID: 2556636

Abstract

Bacteria continuously adapt to changes in their environment. Responses are largely controlled by signal transduction systems that contain two central enzymatic components, a protein kinase that uses adenosine triphosphate to phosphorylate itself at a histidine residue and a response regulator that accepts phosphoryl groups from the kinase. This conserved phosphotransfer chemistry is found in a wide range of bacterial species and operates in diverse systems to provide different regulatory outputs. The histidine kinases are frequently membrane receptor proteins that respond to environmental signals and phosphorylate response regulators that control transcription. Four specific regulatory systems are discussed in detail: chemotaxis in response to attractant and repellent stimuli (Che), regulation of gene expression in response to nitrogen deprivation (Ntr), control of the expression of enzymes and transport systems that assimilate phosphorus (Pho), and regulation of outer membrane porin expression in response to osmolarity and other culture conditions (Omp). Several additional systems are also examined, including systems that control complex developmental processes such as sporulation and fruiting-body formation, systems required for virulent infections of plant or animal host tissues, and systems that regulate transport and metabolism. Finally, an attempt is made to understand how cross-talk between parallel phosphotransfer pathways can provide a global regulatory curcuitry.

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Selected References

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  1. Adler J., Epstein W. Phosphotransferase-system enzymes as chemoreceptors for certain sugars in Escherichia coli chemotaxis. Proc Natl Acad Sci U S A. 1974 Jul;71(7):2895–2899. doi: 10.1073/pnas.71.7.2895. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Adler S. P., Purich D., Stadtman E. R. Cascade control of Escherichia coli glutamine synthetase. Properties of the PII regulatory protein and the uridylyltransferase-uridylyl-removing enzyme. J Biol Chem. 1975 Aug 25;250(16):6264–6272. [PubMed] [Google Scholar]
  3. Aiba H., Mizuno T., Mizushima S. Transfer of phosphoryl group between two regulatory proteins involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli. J Biol Chem. 1989 May 25;264(15):8563–8567. [PubMed] [Google Scholar]
  4. Aiba H., Nakasai F., Mizushima S., Mizuno T. Evidence for the physiological importance of the phosphotransfer between the two regulatory components, EnvZ and OmpR, in osmoregulation in Escherichia coli. J Biol Chem. 1989 Aug 25;264(24):14090–14094. [PubMed] [Google Scholar]
  5. Aiba H., Nakasai F., Mizushima S., Mizuno T. Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in stimulation of its DNA-binding ability. J Biochem. 1989 Jul;106(1):5–7. doi: 10.1093/oxfordjournals.jbchem.a122817. [DOI] [PubMed] [Google Scholar]
  6. Albano M., Hahn J., Dubnau D. Expression of competence genes in Bacillus subtilis. J Bacteriol. 1987 Jul;169(7):3110–3117. doi: 10.1128/jb.169.7.3110-3117.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Albin R., Weber R., Silverman P. M. The Cpx proteins of Escherichia coli K12. Immunologic detection of the chromosomal cpxA gene product. J Biol Chem. 1986 Apr 5;261(10):4698–4705. [PubMed] [Google Scholar]
  8. Alphen W. V., Lugtenberg B. Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli. J Bacteriol. 1977 Aug;131(2):623–630. doi: 10.1128/jb.131.2.623-630.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Alvarez-Morales A., Betancourt-Alvarez M., Kaluza K., Hennecke H. Activation of the Bradyrhizobium japonicum nifH and nifDK operons is dependent on promoter-upstream DNA sequences. Nucleic Acids Res. 1986 May 27;14(10):4207–4227. doi: 10.1093/nar/14.10.4207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ambudkar S. V., Larson T. J., Maloney P. C. Reconstitution of sugar phosphate transport systems of Escherichia coli. J Biol Chem. 1986 Jul 15;261(20):9083–9086. [PubMed] [Google Scholar]
  11. Amemura M., Makino K., Shinagawa H., Kobayashi A., Nakata A. Nucleotide sequence of the genes involved in phosphate transport and regulation of the phosphate regulon in Escherichia coli. J Mol Biol. 1985 Jul 20;184(2):241–250. doi: 10.1016/0022-2836(85)90377-8. [DOI] [PubMed] [Google Scholar]
  12. Amemura M., Makino K., Shinagawa H., Nakata A. Nucleotide sequence of the phoM region of Escherichia coli: four open reading frames may constitute an operon. J Bacteriol. 1986 Oct;168(1):294–302. doi: 10.1128/jb.168.1.294-302.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Ames G. F. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem. 1986;55:397–425. doi: 10.1146/annurev.bi.55.070186.002145. [DOI] [PubMed] [Google Scholar]
  14. Ames P., Parkinson J. S. Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output. Cell. 1988 Dec 2;55(5):817–826. doi: 10.1016/0092-8674(88)90137-7. [DOI] [PubMed] [Google Scholar]
  15. Andersen J., Delihas N., Ikenaka K., Green P. J., Pines O., Ilercil O., Inouye M. The isolation and characterization of RNA coded by the micF gene in Escherichia coli. Nucleic Acids Res. 1987 Mar 11;15(5):2089–2101. doi: 10.1093/nar/15.5.2089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Andersen J., Forst S. A., Zhao K., Inouye M., Delihas N. The function of micF RNA. micF RNA is a major factor in the thermal regulation of OmpF protein in Escherichia coli. J Biol Chem. 1989 Oct 25;264(30):17961–17970. [PubMed] [Google Scholar]
  17. Anthony R. S., Spector L. B. Phosphorylated acetate kinase. Its isolation and reactivity. J Biol Chem. 1972 Apr 10;247(7):2120–2125. [PubMed] [Google Scholar]
  18. Argast M., Boos W. Co-regulation in Escherichia coli of a novel transport system for sn-glycerol-3-phosphate and outer membrane protein Ic (e, E) with alkaline phosphatase and phosphate-binding protein. J Bacteriol. 1980 Jul;143(1):142–150. doi: 10.1128/jb.143.1.142-150.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Armitage J. P., Macnab R. M. Unidirectional, intermittent rotation of the flagellum of Rhodobacter sphaeroides. J Bacteriol. 1987 Feb;169(2):514–518. doi: 10.1128/jb.169.2.514-518.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Armstrong J. B., Adler J., Dahl M. M. Nonchemotactic mutants of Escherichia coli. J Bacteriol. 1967 Jan;93(1):390–398. doi: 10.1128/jb.93.1.390-398.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Aswad D., Koshland D. E., Jr Isolation, characterization and complementation of Salmonella typhimurium chemotaxis mutants. J Mol Biol. 1975 Sep 15;97(2):225–235. doi: 10.1016/s0022-2836(75)80036-2. [DOI] [PubMed] [Google Scholar]
  22. Aswad D., Koshland D. E., Jr Role of methionine in bacterial chemotaxis. J Bacteriol. 1974 May;118(2):640–645. doi: 10.1128/jb.118.2.640-645.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Ausubel F. M. Regulation of nitrogen fixation genes. Cell. 1984 May;37(1):5–6. doi: 10.1016/0092-8674(84)90294-0. [DOI] [PubMed] [Google Scholar]
  24. Aymerich S., Gonzy-Tréboul G., Steinmetz M. 5'-noncoding region sacR is the target of all identified regulation affecting the levansucrase gene in Bacillus subtilis. J Bacteriol. 1986 Jun;166(3):993–998. doi: 10.1128/jb.166.3.993-998.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Ayusawa D., Yoneda Y., Yamane K., Maruo B. Pleiotropic phenomena in autolytic enzyme(s) content, flagellation, and simultaneous hyperproduction of extracellular alpha-amylase and protease in a Bacillus subtilis mutant. J Bacteriol. 1975 Oct;124(1):459–469. doi: 10.1128/jb.124.1.459-469.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Backman K. C., Chen Y. M., Ueno-Nishio S., Magasanik B. The product of glnL is not essential for regulation of bacterial nitrogen assimilation. J Bacteriol. 1983 Apr;154(1):516–519. doi: 10.1128/jb.154.1.516-519.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Backman K., Chen Y. M., Magasanik B. Physical and genetic characterization of the glnA--glnG region of the Escherichia coli chromosome. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3743–3747. doi: 10.1073/pnas.78.6.3743. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Bancroft S., Rhee S. G., Neumann C., Kustu S. Mutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium. J Bacteriol. 1978 Jun;134(3):1046–1055. doi: 10.1128/jb.134.3.1046-1055.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Bartlett D. H., Matsumura P. Identification of Escherichia coli region III flagellar gene products and description of two new flagellar genes. J Bacteriol. 1984 Nov;160(2):577–585. doi: 10.1128/jb.160.2.577-585.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Bassford P. J., Jr, Diedrich D. L., Schnaitman C. L., Reeves P. Outer membrane proteins of Escherichia coli. VI. Protein alteration in bacteriophage-resistant mutants. J Bacteriol. 1977 Aug;131(2):608–622. doi: 10.1128/jb.131.2.608-622.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Bender R. A., Snyder P. M., Bueno R., Quinto M., Magasanik B. Nitrogen regulation system of Klebsiella aerogenes: the nac gene. J Bacteriol. 1983 Oct;156(1):444–446. doi: 10.1128/jb.156.1.444-446.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Bennett R. L., Malamy M. H. Arsenate resistant mutants of Escherichia coli and phosphate transport. Biochem Biophys Res Commun. 1970 Jul 27;40(2):496–503. doi: 10.1016/0006-291x(70)91036-3. [DOI] [PubMed] [Google Scholar]
  33. Benz R., Darveau R. P., Hancock R. E. Outer-membrane protein PhoE from Escherichia coli forms anion-selective pores in lipid-bilayer membranes. Eur J Biochem. 1984 Apr 16;140(2):319–324. doi: 10.1111/j.1432-1033.1984.tb08104.x. [DOI] [PubMed] [Google Scholar]
  34. Berg H. C., Brown D. A. Chemotaxis in Escherichia coli analysed by three-dimensional tracking. Nature. 1972 Oct 27;239(5374):500–504. doi: 10.1038/239500a0. [DOI] [PubMed] [Google Scholar]
  35. Beynon J., Cannon M., Buchanan-Wollaston V., Cannon F. The nif promoters of Klebsiella pneumoniae have a characteristic primary structure. Cell. 1983 Sep;34(2):665–671. doi: 10.1016/0092-8674(83)90399-9. [DOI] [PubMed] [Google Scholar]
  36. Birkmann A., Sawers R. G., Böck A. Involvement of the ntrA gene product in the anaerobic metabolism of Escherichia coli. Mol Gen Genet. 1987 Dec;210(3):535–542. doi: 10.1007/BF00327209. [DOI] [PubMed] [Google Scholar]
  37. Blackhart B. D., Zusman D. R. "Frizzy" genes of Myxococcus xanthus are involved in control of frequency of reversal of gliding motility. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8767–8770. doi: 10.1073/pnas.82.24.8767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Blackhart B. D., Zusman D. R. Cloning and complementation analysis of the "Frizzy" genes of Myxococcus xanthus. Mol Gen Genet. 1985;198(2):243–254. doi: 10.1007/BF00383002. [DOI] [PubMed] [Google Scholar]
  39. Block S. M., Segall J. E., Berg H. C. Impulse responses in bacterial chemotaxis. Cell. 1982 Nov;31(1):215–226. doi: 10.1016/0092-8674(82)90421-4. [DOI] [PubMed] [Google Scholar]
  40. Bloom F. R., Levin M. S., Foor F., Tyler B. Regulation of glutamine synthetase formation in Escherichia coli: characterization of mutants lacking the uridylyltransferase. J Bacteriol. 1978 May;134(2):569–577. doi: 10.1128/jb.134.2.569-577.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Bochner B. R., Ames B. N. Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J Biol Chem. 1982 Aug 25;257(16):9759–9769. [PubMed] [Google Scholar]
  42. Bollinger J., Park C., Harayama S., Hazelbauer G. L. Structure of the Trg protein: Homologies with and differences from other sensory transducers of Escherichia coli. Proc Natl Acad Sci U S A. 1984 Jun;81(11):3287–3291. doi: 10.1073/pnas.81.11.3287. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Borczuk A., Staub A., Stock J. Demethylation of bacterial chemoreceptors is inhibited by attractant stimuli in the complete absence of the regulatory domain of the demethylating enzyme. Biochem Biophys Res Commun. 1986 Dec 30;141(3):918–923. doi: 10.1016/s0006-291x(86)80130-9. [DOI] [PubMed] [Google Scholar]
  44. Borczuk A., Stock A., Stock J. S-adenosylmethionine may not be essential for signal transduction during bacterial chemotaxis. J Bacteriol. 1987 Jul;169(7):3295–3300. doi: 10.1128/jb.169.7.3295-3300.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Borkovich K. A., Kaplan N., Hess J. F., Simon M. I. Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer. Proc Natl Acad Sci U S A. 1989 Feb;86(4):1208–1212. doi: 10.1073/pnas.86.4.1208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Bourret R. B., Hess J. F., Borkovich K. A., Pakula A. A., Simon M. I. Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria. J Biol Chem. 1989 May 5;264(13):7085–7088. [PubMed] [Google Scholar]
  47. Bouvier J., Stragier P., Bonamy C., Szulmajster J. Nucleotide sequence of the spo0B gene of Bacillus subtilis and regulation of its expression. Proc Natl Acad Sci U S A. 1984 Nov;81(22):7012–7016. doi: 10.1073/pnas.81.22.7012. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Bracha M., Yagil E. A ne type of alkaline phosphatase-negative mutants in Escherichia coli K12. Mol Gen Genet. 1973 Mar 27;122(1):53–60. doi: 10.1007/BF00337973. [DOI] [PubMed] [Google Scholar]
  49. Brandl C. J., Green N. M., Korczak B., MacLennan D. H. Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences. Cell. 1986 Feb 28;44(4):597–607. doi: 10.1016/0092-8674(86)90269-2. [DOI] [PubMed] [Google Scholar]
  50. Brenchley J. E., Baker C. A., Patil L. G. Regulation of the ammonia assimilatory enzymes in Salmonella typhimurium. J Bacteriol. 1975 Oct;124(1):182–189. doi: 10.1128/jb.124.1.182-189.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Brickman E., Beckwith J. Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and phi80 transducing phages. J Mol Biol. 1975 Aug 5;96(2):307–316. doi: 10.1016/0022-2836(75)90350-2. [DOI] [PubMed] [Google Scholar]
  52. Buck M. Deletion analysis of the Klebsiella pneumoniae nitrogenase promoter: importance of spacing between conserved sequences around positions -12 and -24 for activation by the nifA and ntrC (glnG) products. J Bacteriol. 1986 May;166(2):545–551. doi: 10.1128/jb.166.2.545-551.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Bueno R., Pahel G., Magasanik B. Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli. J Bacteriol. 1985 Nov;164(2):816–822. doi: 10.1128/jb.164.2.816-822.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Buikema W. J., Szeto W. W., Lemley P. V., Orme-Johnson W. H., Ausubel F. M. Nitrogen fixation specific regulatory genes of Klebsiella pneumoniae and Rhizobium meliloti share homology with the general nitrogen regulatory gene ntrC of K. pneumoniae. Nucleic Acids Res. 1985 Jun 25;13(12):4539–4555. doi: 10.1093/nar/13.12.4539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Case C. C., Bukau B., Granett S., Villarejo M. R., Boos W. Contrasting mechanisms of envZ control of mal and pho regulon genes in Escherichia coli. J Bacteriol. 1986 Jun;166(3):706–712. doi: 10.1128/jb.166.3.706-712.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Cavard D., Pagès J. M., Lazdunski C. Une protéase de la membrane externe d'Escherichia coli sensible aux conditions d'environnement. Ses relations avec l'expression du gène envZ. C R Seances Acad Sci III. 1982 Dec 20;295(13):765–770. [PubMed] [Google Scholar]
  57. Chai T. J., Foulds J. Escherichia coli K-12 tolF mutants: alterations in protein composition of the outer membrane. J Bacteriol. 1977 May;130(2):781–786. doi: 10.1128/jb.130.2.781-786.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Chen C. C., Bruegger B. B., Kern C. W., Lin Y. C., Halpern R. M., Smith R. A. Phosphorylation of nuclear proteins in rat regenerating liver. Biochemistry. 1977 Nov 1;16(22):4852–4855. doi: 10.1021/bi00641a016. [DOI] [PubMed] [Google Scholar]
  59. Chen Y. M., Backman K., Magasanik B. Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli. J Bacteriol. 1982 Apr;150(1):214–220. doi: 10.1128/jb.150.1.214-220.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Chock P. B., Shacter E., Jurgensen S. R., Rhee S. G. Cyclic cascade systems in metabolic regulation. Curr Top Cell Regul. 1985;27:3–12. doi: 10.1016/b978-0-12-152827-0.50008-6. [DOI] [PubMed] [Google Scholar]
  61. Clarke S., Koshland D. E., Jr Membrane receptors for aspartate and serine in bacterial chemotaxis. J Biol Chem. 1979 Oct 10;254(19):9695–9702. [PubMed] [Google Scholar]
  62. Clegg D. O., Koshland D. E., Jr Identification of a bacterial sensing protein and effects of its elevated expression. J Bacteriol. 1985 Apr;162(1):398–405. doi: 10.1128/jb.162.1.398-405.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Collins A. L., Stocker B. A. Salmonella typhimurium mutants generally defective in chemotaxis. J Bacteriol. 1976 Dec;128(3):754–765. doi: 10.1128/jb.128.3.754-765.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Colomb M. G., Chéruy A., Vignais P. V. Nucleoside diphosphokinase from beef heart cytosol. II. Characterization of the phosphorylated intermediate. Biochemistry. 1972 Aug 29;11(18):3378–3386. doi: 10.1021/bi00768a010. [DOI] [PubMed] [Google Scholar]
  65. Comeau D. E., Ikenaka K., Tsung K. L., Inouye M. Primary characterization of the protein products of the Escherichia coli ompB locus: structure and regulation of synthesis of the OmpR and EnvZ proteins. J Bacteriol. 1985 Nov;164(2):578–584. doi: 10.1128/jb.164.2.578-584.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Cornish E. C., Argyropoulos V. P., Pittard J., Davidson B. E. Structure of the Escherichia coli K12 regulatory gene tyrR. Nucleotide sequence and sites of initiation of transcription and translation. J Biol Chem. 1986 Jan 5;261(1):403–410. [PubMed] [Google Scholar]
  67. Csonka L. N. Physiological and genetic responses of bacteria to osmotic stress. Microbiol Rev. 1989 Mar;53(1):121–147. doi: 10.1128/mr.53.1.121-147.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Dame J. B., Scarborough G. A. Identification of the phosphorylated intermediate of the Neurospora plasma membrane H+-ATPase as beta-aspartyl phosphate. J Biol Chem. 1981 Oct 25;256(20):10724–10730. [PubMed] [Google Scholar]
  69. David M., Daveran M. L., Batut J., Dedieu A., Domergue O., Ghai J., Hertig C., Boistard P., Kahn D. Cascade regulation of nif gene expression in Rhizobium meliloti. Cell. 1988 Aug 26;54(5):671–683. doi: 10.1016/s0092-8674(88)80012-6. [DOI] [PubMed] [Google Scholar]
  70. Davies J. K., Reeves P. Genetics of resistance to colicins in Escherichia coli K-12: cross-resistance among colicins of group A. J Bacteriol. 1975 Jul;123(1):102–117. doi: 10.1128/jb.123.1.102-117.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. DeFranco A. L., Koshland D. E., Jr Construction and behavior of strains with mutations in two chemotaxis genes. J Bacteriol. 1982 Jun;150(3):1297–1301. doi: 10.1128/jb.150.3.1297-1301.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. DeFranco A. L., Koshland D. E., Jr Molecular cloning of chemotaxis genes and overproduction of gene products in the bacterial sensing system. J Bacteriol. 1981 Aug;147(2):390–400. doi: 10.1128/jb.147.2.390-400.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Dean G. E., Aizawa S. I., Macnab R. M. flaAII (motC, cheV) of Salmonella typhimurium is a structural gene involved in energization and switching of the flagellar motor. J Bacteriol. 1983 Apr;154(1):84–91. doi: 10.1128/jb.154.1.84-91.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Degani C., Boyer P. D. A borohydride reduction method for characterization of the acyl phosphate linkage in proteins and its application to sarcoplasmic reticulum adenosine triphosphatase. J Biol Chem. 1973 Dec 10;248(23):8222–8226. [PubMed] [Google Scholar]
  75. Deretic V., Dikshit R., Konyecsni W. M., Chakrabarty A. M., Misra T. K. The algR gene, which regulates mucoidy in Pseudomonas aeruginosa, belongs to a class of environmentally responsive genes. J Bacteriol. 1989 Mar;171(3):1278–1283. doi: 10.1128/jb.171.3.1278-1283.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Deretic V., Konyecsni W. M. Control of mucoidy in Pseudomonas aeruginosa: transcriptional regulation of algR and identification of the second regulatory gene, algQ. J Bacteriol. 1989 Jul;171(7):3680–3688. doi: 10.1128/jb.171.7.3680-3688.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. DiRienzo J. M., Inouye M. Lipid fluidity-dependent biosynthesis and assembly of the outer membrane proteins of E. coli. Cell. 1979 May;17(1):155–161. doi: 10.1016/0092-8674(79)90303-9. [DOI] [PubMed] [Google Scholar]
  78. Dietz G. W., Heppel L. A. Studies on the uptake of hexose phosphates. II. The induction of the glucose 6-phosphate transport system by exogenous but not by endogenously formed glucose 6-phosphate. J Biol Chem. 1971 May 10;246(9):2885–2890. [PubMed] [Google Scholar]
  79. Dixon R. A. The genetic complexity of nitrogen fixation. The ninth Fleming lecture. J Gen Microbiol. 1984 Nov;130(11):2745–2755. doi: 10.1099/00221287-130-11-2745. [DOI] [PubMed] [Google Scholar]
  80. Dixon R. The xylABC promoter from the Pseudomonas putida TOL plasmid is activated by nitrogen regulatory genes in Escherichia coli. Mol Gen Genet. 1986 Apr;203(1):129–136. doi: 10.1007/BF00330393. [DOI] [PubMed] [Google Scholar]
  81. Drummond M. H., Wootton J. C. Sequence of nifL from Klebsiella pneumoniae: mode of action and relationship to two families of regulatory proteins. Mol Microbiol. 1987 Jul;1(1):37–44. doi: 10.1111/j.1365-2958.1987.tb00524.x. [DOI] [PubMed] [Google Scholar]
  82. Drummond M., Clements J., Merrick M., Dixon R. Positive control and autogenous regulation of the nifLA promoter in Klebsiella pneumoniae. Nature. 1983 Jan 27;301(5898):302–307. doi: 10.1038/301302a0. [DOI] [PubMed] [Google Scholar]
  83. Drummond M., Whitty P., Wootton J. Sequence and domain relationships of ntrC and nifA from Klebsiella pneumoniae: homologies to other regulatory proteins. EMBO J. 1986 Feb;5(2):441–447. doi: 10.1002/j.1460-2075.1986.tb04230.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Drury L. S., Buxton R. S. DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins. J Biol Chem. 1985 Apr 10;260(7):4236–4242. [PubMed] [Google Scholar]
  85. Edlund B., Rask L., Olsson P., Wålinder O., Zetterqvist O., Engström L. Preparation of crystalline nucleoside diphosphate kinase from baker's yeast and identification of 1-[32P]phosphohistidine as the main phosphorylated product of an alkaline hydrolysate of enzyme incubated with adenosine [32P]triphosphate. Eur J Biochem. 1969 Jul;9(4):451–455. doi: 10.1111/j.1432-1033.1969.tb00630.x. [DOI] [PubMed] [Google Scholar]
  86. Enomoto M. Genetic studies of paralyzed mutant in Salmonella. I. Genetic fine structure of the mot loci in Salmonella typhimurium. Genetics. 1966 Sep;54(3):715–726. doi: 10.1093/genetics/54.3.715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  87. Feldman F., Butler L. G. Protein-bound phosphoryl histidine: a probable intermediate in the microsomal glucose-6-phosphatase-inorganic pyrophosphatase reaction. Biochim Biophys Acta. 1972 Jun 16;268(3):698–710. doi: 10.1016/0005-2744(72)90274-4. [DOI] [PubMed] [Google Scholar]
  88. Ferrari F. A., Trach K., LeCoq D., Spence J., Ferrari E., Hoch J. A. Characterization of the spo0A locus and its deduced product. Proc Natl Acad Sci U S A. 1985 May;82(9):2647–2651. doi: 10.1073/pnas.82.9.2647. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Ferro-Luzzi Ames G., Nikaido K. Nitrogen regulation in Salmonella typhimurium. Identification of an ntrC protein-binding site and definition of a consensus binding sequence. EMBO J. 1985 Feb;4(2):539–547. doi: 10.1002/j.1460-2075.1985.tb03662.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Fields P. I., Groisman E. A., Heffron F. A Salmonella locus that controls resistance to microbicidal proteins from phagocytic cells. Science. 1989 Feb 24;243(4894 Pt 1):1059–1062. doi: 10.1126/science.2646710. [DOI] [PubMed] [Google Scholar]
  91. Fields P. I., Swanson R. V., Haidaris C. G., Heffron F. Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5189–5193. doi: 10.1073/pnas.83.14.5189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  92. Flynn J. L., Ohman D. E. Cloning of genes from mucoid Pseudomonas aeruginosa which control spontaneous conversion to the alginate production phenotype. J Bacteriol. 1988 Apr;170(4):1452–1460. doi: 10.1128/jb.170.4.1452-1460.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  93. Flynn J. L., Ohman D. E. Use of a gene replacement cosmid vector for cloning alginate conversion genes from mucoid and nonmucoid Pseudomonas aeruginosa strains: algS controls expression of algT. J Bacteriol. 1988 Jul;170(7):3228–3236. doi: 10.1128/jb.170.7.3228-3236.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Foor F., Cedergren R. J., Streicher S. L., Rhee S. G., Magasanik B. Glutamine synthetase of Klebsiella aerogenes: properties of glnD mutants lacking uridylyltransferase. J Bacteriol. 1978 May;134(2):562–568. doi: 10.1128/jb.134.2.562-568.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Foor F., Reuveny Z., Magasanik B. Regulation of the synthesis of glutamine synthetase by the PII protein in Klebsiella aerogenes. Proc Natl Acad Sci U S A. 1980 May;77(5):2636–2640. doi: 10.1073/pnas.77.5.2636. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Forst S., Comeau D., Norioka S., Inouye M. Localization and membrane topology of EnvZ, a protein involved in osmoregulation of OmpF and OmpC in Escherichia coli. J Biol Chem. 1987 Dec 5;262(34):16433–16438. [PubMed] [Google Scholar]
  97. Forst S., Delgado J., Inouye M. Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6052–6056. doi: 10.1073/pnas.86.16.6052. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. Forst S., Delgado J., Ramakrishnan G., Inouye M. Regulation of ompC and ompF expression in Escherichia coli in the absence of envZ. J Bacteriol. 1988 Nov;170(11):5080–5085. doi: 10.1128/jb.170.11.5080-5085.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Forst S., Inouye M. Environmentally regulated gene expression for membrane proteins in Escherichia coli. Annu Rev Cell Biol. 1988;4:21–42. doi: 10.1146/annurev.cb.04.110188.000321. [DOI] [PubMed] [Google Scholar]
  100. Foulds J., Barrett C. Characterization of Escherichia coli mutants tolerant to bacteriocin JF246: two new classes of tolerant mutants. J Bacteriol. 1973 Nov;116(2):885–892. doi: 10.1128/jb.116.2.885-892.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  101. Fox D. K., Meadow N. D., Roseman S. Phosphate transfer between acetate kinase and enzyme I of the bacterial phosphotransferase system. J Biol Chem. 1986 Oct 15;261(29):13498–13503. [PubMed] [Google Scholar]
  102. Friedrich M. J., Kadner R. J. Nucleotide sequence of the uhp region of Escherichia coli. J Bacteriol. 1987 Aug;169(8):3556–3563. doi: 10.1128/jb.169.8.3556-3563.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Gaillardin C. M., Magasanik B. Involvement of the product of the glnF gene in the autogenous regulation of glutamine synthetase formation in Klebsiella aerogenes. J Bacteriol. 1978 Mar;133(3):1329–1338. doi: 10.1128/jb.133.3.1329-1338.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Garcia E., Bancroft S., Rhee S. G., Kustu S. The product of a newly identified gene, gInF, is required for synthesis of glutamine synthetase in Salmonella. Proc Natl Acad Sci U S A. 1977 Apr;74(4):1662–1666. doi: 10.1073/pnas.74.4.1662. [DOI] [PMC free article] [PubMed] [Google Scholar]
  105. Garcia E., Rhee S. G. Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII uridylyltransferase and uridylyl-removing enzyme. J Biol Chem. 1983 Feb 25;258(4):2246–2253. [PubMed] [Google Scholar]
  106. Garrett S., Silhavy T. J. Isolation of mutations in the alpha operon of Escherichia coli that suppress the transcriptional defect conferred by a mutation in the porin regulatory gene envZ. J Bacteriol. 1987 Apr;169(4):1379–1385. doi: 10.1128/jb.169.4.1379-1385.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. Garrett S., Taylor R. K., Silhavy T. J. Isolation and characterization of chain-terminating nonsense mutations in a porin regulator gene, envZ. J Bacteriol. 1983 Oct;156(1):62–69. doi: 10.1128/jb.156.1.62-69.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Gibson M. M., Ellis E. M., Graeme-Cook K. A., Higgins C. F. OmpR and EnvZ are pleiotropic regulatory proteins: positive regulation of the tripeptide permease (tppB) of Salmonella typhimurium. Mol Gen Genet. 1987 Apr;207(1):120–129. doi: 10.1007/BF00331499. [DOI] [PubMed] [Google Scholar]
  109. Goldrick D., Yu G. Q., Jiang S. Q., Hong J. S. Nucleotide sequence and transcription start point of the phosphoglycerate transporter gene of Salmonella typhimurium. J Bacteriol. 1988 Aug;170(8):3421–3426. doi: 10.1128/jb.170.8.3421-3426.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. Goy M. F., Springer M. S., Adler J. Failure of sensory adaptation in bacterial mutants that are defective in a protein methylation reaction. Cell. 1978 Dec;15(4):1231–1240. doi: 10.1016/0092-8674(78)90049-1. [DOI] [PubMed] [Google Scholar]
  111. Goy M. F., Springer M. S., Adler J. Sensory transduction in Escherichia coli: role of a protein methylation reaction in sensory adaptation. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4964–4968. doi: 10.1073/pnas.74.11.4964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. Guan C. D., Wanner B., Inouye H. Analysis of regulation of phoB expression using a phoB-cat fusion. J Bacteriol. 1983 Nov;156(2):710–717. doi: 10.1128/jb.156.2.710-717.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  113. Gussin G. N., Ronson C. W., Ausubel F. M. Regulation of nitrogen fixation genes. Annu Rev Genet. 1986;20:567–591. doi: 10.1146/annurev.ge.20.120186.003031. [DOI] [PubMed] [Google Scholar]
  114. Götz R., Schmitt R. Rhizobium meliloti swims by unidirectional, intermittent rotation of right-handed flagellar helices. J Bacteriol. 1987 Jul;169(7):3146–3150. doi: 10.1128/jb.169.7.3146-3150.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. Hahn J., Albano M., Dubnau D. Isolation and characterization of Tn917lac-generated competence mutants of Bacillus subtilis. J Bacteriol. 1987 Jul;169(7):3104–3109. doi: 10.1128/jb.169.7.3104-3109.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  116. Hall M. N., Silhavy T. J. Genetic analysis of the ompB locus in Escherichia coli K-12. J Mol Biol. 1981 Sep 5;151(1):1–15. doi: 10.1016/0022-2836(81)90218-7. [DOI] [PubMed] [Google Scholar]
  117. Hall M. N., Silhavy T. J. The ompB locus and the regulation of the major outer membrane porin proteins of Escherichia coli K12. J Mol Biol. 1981 Feb 15;146(1):23–43. doi: 10.1016/0022-2836(81)90364-8. [DOI] [PubMed] [Google Scholar]
  118. Hall M. N., Silhavy T. J. Transcriptional regulation of Escherichia coli K-12 major outer membrane protein 1b. J Bacteriol. 1979 Nov;140(2):342–350. doi: 10.1128/jb.140.2.342-350.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  119. Hancock R. E. Role of porins in outer membrane permeability. J Bacteriol. 1987 Mar;169(3):929–933. doi: 10.1128/jb.169.3.929-933.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. Hawkes T., Merrick M., Dixon R. Interaction of purified NtrC protein with nitrogen regulated promoters from Klebsiella pneumoniae. Mol Gen Genet. 1985;201(3):492–498. doi: 10.1007/BF00331345. [DOI] [PubMed] [Google Scholar]
  121. Henner D. J., Ferrari E., Perego M., Hoch J. A. Location of the targets of the hpr-97, sacU32(Hy), and sacQ36(Hy) mutations in upstream regions of the subtilisin promoter. J Bacteriol. 1988 Jan;170(1):296–300. doi: 10.1128/jb.170.1.296-300.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  122. Henner D. J., Yang M., Ferrari E. Localization of Bacillus subtilis sacU(Hy) mutations to two linked genes with similarities to the conserved procaryotic family of two-component signalling systems. J Bacteriol. 1988 Nov;170(11):5102–5109. doi: 10.1128/jb.170.11.5102-5109.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Hess J. F., Bourret R. B., Simon M. I. Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis. Nature. 1988 Nov 10;336(6195):139–143. doi: 10.1038/336139a0. [DOI] [PubMed] [Google Scholar]
  124. Hess J. F., Oosawa K., Kaplan N., Simon M. I. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell. 1988 Apr 8;53(1):79–87. doi: 10.1016/0092-8674(88)90489-8. [DOI] [PubMed] [Google Scholar]
  125. Hess J. F., Oosawa K., Matsumura P., Simon M. I. Protein phosphorylation is involved in bacterial chemotaxis. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7609–7613. doi: 10.1073/pnas.84.21.7609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  126. Hesse J. E., Wieczorek L., Altendorf K., Reicin A. S., Dorus E., Epstein W. Sequence homology between two membrane transport ATPases, the Kdp-ATPase of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4746–4750. doi: 10.1073/pnas.81.15.4746. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Higgins C. F., Ames G. F. Regulatory regions of two transport operons under nitrogen control: nucleotide sequences. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1083–1087. doi: 10.1073/pnas.79.4.1083. [DOI] [PMC free article] [PubMed] [Google Scholar]
  128. Hill S., Kennedy C., Kavanagh E., Goldberg R. B., Hanau R. Nitrogen fixation gene (nifL) involved in oxygen regulation of nitrogenase synthesis in K. pneumoniae. Nature. 1981 Apr 2;290(5805):424–426. doi: 10.1038/290424a0. [DOI] [PubMed] [Google Scholar]
  129. Hirota N., Imae Y. Na+-driven flagellar motors of an alkalophilic Bacillus strain YN-1. J Biol Chem. 1983 Sep 10;258(17):10577–10581. [PubMed] [Google Scholar]
  130. Hirschman J., Wong P. K., Sei K., Keener J., Kustu S. Products of nitrogen regulatory genes ntrA and ntrC of enteric bacteria activate glnA transcription in vitro: evidence that the ntrA product is a sigma factor. Proc Natl Acad Sci U S A. 1985 Nov;82(22):7525–7529. doi: 10.1073/pnas.82.22.7525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  131. Hoch J. A., Trach K., Kawamura F., Saito H. Identification of the transcriptional suppressor sof-1 as an alteration in the spo0A protein. J Bacteriol. 1985 Feb;161(2):552–555. doi: 10.1128/jb.161.2.552-555.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  132. Homma M., Iino T., Macnab R. M. Identification and characterization of the products of six region III flagellar genes (flaAII.3 through flaQII) of Salmonella typhimurium. J Bacteriol. 1988 May;170(5):2221–2228. doi: 10.1128/jb.170.5.2221-2228.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. Hunt T. P., Magasanik B. Transcription of glnA by purified Escherichia coli components: core RNA polymerase and the products of glnF, glnG, and glnL. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8453–8457. doi: 10.1073/pnas.82.24.8453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  134. Ichihara S., Mizushima S. Characterization of major outer membrane proteins O-8 and O-9 of Escherichia coli K-12. Evidence that structural genes for the two proteins are different. J Biochem. 1978 Apr;83(4):1095–1100. doi: 10.1093/oxfordjournals.jbchem.a131998. [DOI] [PubMed] [Google Scholar]
  135. Igo M. M., Ninfa A. J., Silhavy T. J. A bacterial environmental sensor that functions as a protein kinase and stimulates transcriptional activation. Genes Dev. 1989 May;3(5):598–605. doi: 10.1101/gad.3.5.598. [DOI] [PubMed] [Google Scholar]
  136. Igo M. M., Ninfa A. J., Stock J. B., Silhavy T. J. Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 1989 Nov;3(11):1725–1734. doi: 10.1101/gad.3.11.1725. [DOI] [PubMed] [Google Scholar]
  137. Igo M. M., Silhavy T. J. EnvZ, a transmembrane environmental sensor of Escherichia coli K-12, is phosphorylated in vitro. J Bacteriol. 1988 Dec;170(12):5971–5973. doi: 10.1128/jb.170.12.5971-5973.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  138. Iino T., Komeda Y., Kutsukake K., Macnab R. M., Matsumura P., Parkinson J. S., Simon M. I., Yamaguchi S. New unified nomenclature for the flagellar genes of Escherichia coli and Salmonella typhimurium. Microbiol Rev. 1988 Dec;52(4):533–535. doi: 10.1128/mr.52.4.533-535.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  139. Ikenaka K., Tsung K., Comeau D. E., Inouye M. A dominant mutation in Escherichia coli OmpR lies within a domain which is highly conserved in a large family of bacterial regulatory proteins. Mol Gen Genet. 1988 Mar;211(3):538–540. doi: 10.1007/BF00425713. [DOI] [PubMed] [Google Scholar]
  140. Ikeuchi T., Kudoh J., Tsunasawa S. Amino-terminal structure of spoOA protein and sequence homology with spoOF and spoOB proteins. Mol Gen Genet. 1986 Jun;203(3):371–376. doi: 10.1007/BF00422059. [DOI] [PubMed] [Google Scholar]
  141. Ikeuchi T., Tsunasawa S., Sakiyama F. Purification and characterization of the spoOA protein of Bacillus subtilis from an overproducing strain of Escherichia coli. Eur J Biochem. 1987 Sep 1;167(2):233–238. doi: 10.1111/j.1432-1033.1987.tb13328.x. [DOI] [PubMed] [Google Scholar]
  142. Inokuchi K., Furukawa H., Nakamura K., Mizushima S. Characterization by deletion mutagenesis in vitro of the promoter region of ompF, a positively regulated gene of Escherichia coli. J Mol Biol. 1984 Sep 25;178(3):653–668. doi: 10.1016/0022-2836(84)90243-2. [DOI] [PubMed] [Google Scholar]
  143. Inouye S., Ebina Y., Nakazawa A., Nakazawa T. Nucleotide sequence surrounding transcription initiation site of xylABC operon on TOL plasmid of Pseudomonas putida. Proc Natl Acad Sci U S A. 1984 Mar;81(6):1688–1691. doi: 10.1073/pnas.81.6.1688. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Ito K., Sato T., Yura T. Synthesis and assembly of the membrane proteins in E. coli. Cell. 1977 Jul;11(3):551–559. doi: 10.1016/0092-8674(77)90073-3. [DOI] [PubMed] [Google Scholar]
  145. Iuchi S., Cameron D. C., Lin E. C. A second global regulator gene (arcB) mediating repression of enzymes in aerobic pathways of Escherichia coli. J Bacteriol. 1989 Feb;171(2):868–873. doi: 10.1128/jb.171.2.868-873.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  146. Iuchi S., Lin E. C. The narL gene product activates the nitrate reductase operon and represses the fumarate reductase and trimethylamine N-oxide reductase operons in Escherichia coli. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3901–3905. doi: 10.1073/pnas.84.11.3901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  147. Iuchi S., Lin E. C. arcA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1888–1892. doi: 10.1073/pnas.85.6.1888. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Jamieson D. J., Higgins C. F. Anaerobic and leucine-dependent expression of a peptide transport gene in Salmonella typhimurium. J Bacteriol. 1984 Oct;160(1):131–136. doi: 10.1128/jb.160.1.131-136.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Jencks W. P. The utilization of binding energy in coupled vectorial processes. Adv Enzymol Relat Areas Mol Biol. 1980;51:75–106. doi: 10.1002/9780470122969.ch2. [DOI] [PubMed] [Google Scholar]
  150. Jiang S. Q., Yu G. Q., Li Z. G., Hong J. S. Genetic evidence for modulation of the activator by two regulatory proteins involved in the exogenous induction of phosphoglycerate transport in Salmonella typhimurium. J Bacteriol. 1988 Sep;170(9):4304–4308. doi: 10.1128/jb.170.9.4304-4308.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Jo Y. L., Nara F., Ichihara S., Mizuno T., Mizushima S. Purification and characterization of the OmpR protein, a positive regulator involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli. J Biol Chem. 1986 Nov 15;261(32):15252–15256. [PubMed] [Google Scholar]
  152. Kawaji H., Mizuno T., Mizushima S. Influence of molecular size and osmolarity of sugars and dextrans on the synthesis of outer membrane proteins O-8 and O-9 of Escherichia coli K-12. J Bacteriol. 1979 Dec;140(3):843–847. doi: 10.1128/jb.140.3.843-847.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  153. Keener J., Kustu S. Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: roles of the conserved amino-terminal domain of NTRC. Proc Natl Acad Sci U S A. 1988 Jul;85(14):4976–4980. doi: 10.1073/pnas.85.14.4976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. Kehry M. R., Bond M. W., Hunkapiller M. W., Dahlquist F. W. Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product. Proc Natl Acad Sci U S A. 1983 Jun;80(12):3599–3603. doi: 10.1073/pnas.80.12.3599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. Kehry M. R., Dahlquist F. W. Adaptation in bacterial chemotaxis: CheB-dependent modification permits additional methylations of sensory transducer proteins. Cell. 1982 Jul;29(3):761–772. doi: 10.1016/0092-8674(82)90438-x. [DOI] [PubMed] [Google Scholar]
  156. Kehry M. R., Dahlquist F. W. The methyl-accepting chemotaxis proteins of Escherichia coli. Identification of the multiple methylation sites on methyl-accepting chemotaxis protein I. J Biol Chem. 1982 Sep 10;257(17):10378–10386. [PubMed] [Google Scholar]
  157. Kehry M. R., Doak T. G., Dahlquist F. W. Sensory adaptation in bacterial chemotaxis: regulation of demethylation. J Bacteriol. 1985 Sep;163(3):983–990. doi: 10.1128/jb.163.3.983-990.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  158. Kehry M. R., Doak T. G., Dahlquist F. W. Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli. J Biol Chem. 1984 Oct 10;259(19):11828–11835. [PubMed] [Google Scholar]
  159. Kehry M. R., Engström P., Dahlquist F. W., Hazelbauer G. L. Multiple covalent modifications of Trg, a sensory transducer of Escherichia coli. J Biol Chem. 1983 Apr 25;258(8):5050–5055. [PubMed] [Google Scholar]
  160. Khan S., Macnab R. M., DeFranco A. L., Koshland D. E., Jr Inversion of a behavioral response in bacterial chemotaxis: explanation at the molecular level. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4150–4154. doi: 10.1073/pnas.75.9.4150. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. Kier L. D., Weppelman R. M., Ames B. N. Regulation of nonspecific acid phosphatase in Salmonella: phoN and phoP genes. J Bacteriol. 1979 Apr;138(1):155–161. doi: 10.1128/jb.138.1.155-161.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  162. Kikuchi Y., Yoda K., Yamasaki M., Tamura G. The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli. Nucleic Acids Res. 1981 Nov 11;9(21):5671–5678. doi: 10.1093/nar/9.21.5671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  163. Kofoid E. C., Parkinson J. S. Transmitter and receiver modules in bacterial signaling proteins. Proc Natl Acad Sci U S A. 1988 Jul;85(14):4981–4985. doi: 10.1073/pnas.85.14.4981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. Krajewska-Grynkiewicz K., Kustu S. Evidence that nitrogen regulatory gene ntrC of Salmonella typhimurium is transcribed from the glnA promoter as well as from a separate ntr promoter. Mol Gen Genet. 1984;193(1):135–142. doi: 10.1007/BF00327426. [DOI] [PubMed] [Google Scholar]
  165. Kreil G., Boyer P. D. Detection of bound phosphohistidine in E. coli succinate thiokinase. Biochem Biophys Res Commun. 1964 Aug 11;16(6):551–555. doi: 10.1016/0006-291x(64)90191-3. [DOI] [PubMed] [Google Scholar]
  166. Krikos A., Conley M. P., Boyd A., Berg H. C., Simon M. I. Chimeric chemosensory transducers of Escherichia coli. Proc Natl Acad Sci U S A. 1985 Mar;82(5):1326–1330. doi: 10.1073/pnas.82.5.1326. [DOI] [PMC free article] [PubMed] [Google Scholar]
  167. Krikos A., Mutoh N., Boyd A., Simon M. I. Sensory transducers of E. coli are composed of discrete structural and functional domains. Cell. 1983 Jun;33(2):615–622. doi: 10.1016/0092-8674(83)90442-7. [DOI] [PubMed] [Google Scholar]
  168. Kröger M. Compilation of DNA sequences of Escherichia coli. Nucleic Acids Res. 1989;17 (Suppl):r283–r309. doi: 10.1093/nar/17.suppl.r283. [DOI] [PMC free article] [PubMed] [Google Scholar]
  169. Kunst F., Debarbouille M., Msadek T., Young M., Mauel C., Karamata D., Klier A., Rapoport G., Dedonder R. Deduced polypeptides encoded by the Bacillus subtilis sacU locus share homology with two-component sensor-regulator systems. J Bacteriol. 1988 Nov;170(11):5093–5101. doi: 10.1128/jb.170.11.5093-5101.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  170. Kunst F., Pascal M., Lepesant-Kejzlarova J., Lepesant J. A., Billault A., Dedonder R. Pleiotropic mutations affecting sporulation conditions and the syntheses of extracellular enzymes in Bacillus subtilis 168. Biochimie. 1974;56(11-12):1481–1489. doi: 10.1016/s0300-9084(75)80270-7. [DOI] [PubMed] [Google Scholar]
  171. Kuo S. C., Koshland D. E., Jr Roles of cheY and cheZ gene products in controlling flagellar rotation in bacterial chemotaxis of Escherichia coli. J Bacteriol. 1987 Mar;169(3):1307–1314. doi: 10.1128/jb.169.3.1307-1314.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Kuo S. C., Koshland D. E., Jr Sequence of the flaA (cheC) locus of Escherichia coli and discovery of a new gene. J Bacteriol. 1986 Jun;166(3):1007–1012. doi: 10.1128/jb.166.3.1007-1012.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  173. Kustu S. G., McFarland N. C., Hui S. P., Esmon B., Ames G. F. Nitrogen control of Salmonella typhimurium: co-regulation of synthesis of glutamine synthetase and amino acid transport systems. J Bacteriol. 1979 Apr;138(1):218–234. doi: 10.1128/jb.138.1.218-234.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  174. Kustu S. G., McKereghan K. Mutations affecting glutamine synthetase activity in Salmonella typhimurium. J Bacteriol. 1975 Jun;122(3):1006–1016. doi: 10.1128/jb.122.3.1006-1016.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  175. Kustu S., Burton D., Garcia E., McCarter L., McFarland N. Nitrogen control in Salmonella: regulation by the glnR and glnF gene products. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4576–4580. doi: 10.1073/pnas.76.9.4576. [DOI] [PMC free article] [PubMed] [Google Scholar]
  176. Kustu S., Santero E., Keener J., Popham D., Weiss D. Expression of sigma 54 (ntrA)-dependent genes is probably united by a common mechanism. Microbiol Rev. 1989 Sep;53(3):367–376. doi: 10.1128/mr.53.3.367-376.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  177. Lapidus I. R., Welch M., Eisenbach M. Pausing of flagellar rotation is a component of bacterial motility and chemotaxis. J Bacteriol. 1988 Aug;170(8):3627–3632. doi: 10.1128/jb.170.8.3627-3632.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  178. Larsen S. H., Adler J., Gargus J. J., Hogg R. W. Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1239–1243. doi: 10.1073/pnas.71.4.1239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  179. Leroux B., Yanofsky M. F., Winans S. C., Ward J. E., Ziegler S. F., Nester E. W. Characterization of the virA locus of Agrobacterium tumefaciens: a transcriptional regulator and host range determinant. EMBO J. 1987 Apr;6(4):849–856. doi: 10.1002/j.1460-2075.1987.tb04830.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  180. Lewandoski M., Dubnau E., Smith I. Transcriptional regulation of the spo0F gene of Bacillus subtilis. J Bacteriol. 1986 Nov;168(2):870–877. doi: 10.1128/jb.168.2.870-877.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  181. Li S. F., DeMoss J. A. Location of sequences in the nar promoter of Escherichia coli required for regulation by Fnr and NarL. J Biol Chem. 1988 Sep 25;263(27):13700–13705. [PubMed] [Google Scholar]
  182. Liljeström P., Luokkamäki M., Palva E. T. Isolation and characterization of a substitution mutation in the ompR gene of Salmonella typhimurium LT2. J Bacteriol. 1987 Jan;169(1):438–441. doi: 10.1128/jb.169.1.438-441.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  183. Losick R., Youngman P., Piggot P. J. Genetics of endospore formation in Bacillus subtilis. Annu Rev Genet. 1986;20:625–669. doi: 10.1146/annurev.ge.20.120186.003205. [DOI] [PubMed] [Google Scholar]
  184. Luckey M., Nikaido H. Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli: inhibition by higher oligosaccharides of maltose series. Biochem Biophys Res Commun. 1980 Mar 13;93(1):166–171. doi: 10.1016/s0006-291x(80)80261-0. [DOI] [PubMed] [Google Scholar]
  185. Luckey M., Nikaido H. Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. Proc Natl Acad Sci U S A. 1980 Jan;77(1):167–171. doi: 10.1073/pnas.77.1.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  186. Ludtke D., Bernstein J., Hamilton C., Torriani A. Identification of the phoM gene product and its regulation in Escherichia coli K-12. J Bacteriol. 1984 Jul;159(1):19–25. doi: 10.1128/jb.159.1.19-25.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  187. Lugtenberg B., Peters R., Bernheimer H., Berendsen W. Influence of cultural conditions and mutations on the composition of the outer membrane proteins of Escherichia coli. Mol Gen Genet. 1976 Sep 23;147(3):251–262. doi: 10.1007/BF00582876. [DOI] [PubMed] [Google Scholar]
  188. Lundrigan M., Earhart C. F. Reduction in three iron-regulated outer membrane proteins and protein a by the Escherichia coli K-12 perA mutation. J Bacteriol. 1981 May;146(2):804–807. doi: 10.1128/jb.146.2.804-807.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  189. Lupas A., Stock J. Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis. J Biol Chem. 1989 Oct 15;264(29):17337–17342. [PubMed] [Google Scholar]
  190. MacFarlane S. A., Merrick M. The nucleotide sequence of the nitrogen regulation gene ntrB and the glnA-ntrBC intergenic region of Klebsiella pneumoniae. Nucleic Acids Res. 1985 Nov 11;13(21):7591–7606. doi: 10.1093/nar/13.21.7591. [DOI] [PMC free article] [PubMed] [Google Scholar]
  191. MacFarlane S. A., Merrick M. The nucleotide sequence of the nitrogen regulation gene ntrB and the glnA-ntrBC intergenic region of Klebsiella pneumoniae. Nucleic Acids Res. 1985 Nov 11;13(21):7591–7606. doi: 10.1093/nar/13.21.7591. [DOI] [PMC free article] [PubMed] [Google Scholar]
  192. MacLennan D. H., Brandl C. J., Korczak B., Green N. M. Amino-acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature. 1985 Aug 22;316(6030):696–700. doi: 10.1038/316696a0. [DOI] [PubMed] [Google Scholar]
  193. MacNeil T., Roberts G. P., MacNeil D., Tyler B. The products of glnL and glnG are bifunctional regulatory proteins. Mol Gen Genet. 1982;188(2):325–333. doi: 10.1007/BF00332696. [DOI] [PubMed] [Google Scholar]
  194. Macnab R. M., Koshland D. E., Jr The gradient-sensing mechanism in bacterial chemotaxis. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2509–2512. doi: 10.1073/pnas.69.9.2509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  195. Macnab R. M., Ornston M. K. Normal-to-curly flagellar transitions and their role in bacterial tumbling. Stabilization of an alternative quaternary structure by mechanical force. J Mol Biol. 1977 May 5;112(1):1–30. doi: 10.1016/s0022-2836(77)80153-8. [DOI] [PubMed] [Google Scholar]
  196. Maeda S., Mizuno T. Activation of the ompC gene by the OmpR protein in Escherichia coli. The cis-acting upstream sequence can function in both orientations with respect to the canonical promoter. J Biol Chem. 1988 Oct 15;263(29):14629–14633. [PubMed] [Google Scholar]
  197. Magasanik B. Genetic control of nitrogen assimilation in bacteria. Annu Rev Genet. 1982;16:135–168. doi: 10.1146/annurev.ge.16.120182.001031. [DOI] [PubMed] [Google Scholar]
  198. Magasanik B. Reversible phosphorylation of an enhancer binding protein regulates the transcription of bacterial nitrogen utilization genes. Trends Biochem Sci. 1988 Dec;13(12):475–479. doi: 10.1016/0968-0004(88)90234-4. [DOI] [PubMed] [Google Scholar]
  199. Magota K., Otsuji N., Miki T., Horiuchi T., Tsunasawa S., Kondo J., Sakiyama F., Amemura M., Morita T., Shinagawa H. Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli. J Bacteriol. 1984 Mar;157(3):909–917. doi: 10.1128/jb.157.3.909-917.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  200. Makino K., Shinagawa H., Amemura M., Kimura S., Nakata A., Ishihama A. Regulation of the phosphate regulon of Escherichia coli. Activation of pstS transcription by PhoB protein in vitro. J Mol Biol. 1988 Sep 5;203(1):85–95. doi: 10.1016/0022-2836(88)90093-9. [DOI] [PubMed] [Google Scholar]
  201. Makino K., Shinagawa H., Amemura M., Nakata A. Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12. J Mol Biol. 1986 Jul 5;190(1):37–44. doi: 10.1016/0022-2836(86)90073-2. [DOI] [PubMed] [Google Scholar]
  202. Makino K., Shinagawa H., Amemura M., Nakata A. Nucleotide sequence of the phoR gene, a regulatory gene for the phosphate regulon of Escherichia coli. J Mol Biol. 1986 Dec 5;192(3):549–556. doi: 10.1016/0022-2836(86)90275-5. [DOI] [PubMed] [Google Scholar]
  203. Makino K., Shinagawa H., Nakata A. Cloning and characterization of the alkaline phosphatase positive regulatory gene (phoM) of Escherichia coli. Mol Gen Genet. 1984;195(3):381–390. doi: 10.1007/BF00341438. [DOI] [PubMed] [Google Scholar]
  204. Makino K., Shinagawa H., Nakata A. Regulation of the phosphate regulon of Escherichia coli K-12: regulation and role of the regulatory gene phoR. J Mol Biol. 1985 Jul 20;184(2):231–240. doi: 10.1016/0022-2836(85)90376-6. [DOI] [PubMed] [Google Scholar]
  205. Mallonee D. H., Glatz B. A., Pattee P. A. Chromosomal mapping of a gene affecting enterotoxin A production in Staphylococcus aureus. Appl Environ Microbiol. 1982 Feb;43(2):397–402. doi: 10.1128/aem.43.2.397-402.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  206. Manoil C., Beckwith J. A genetic approach to analyzing membrane protein topology. Science. 1986 Sep 26;233(4771):1403–1408. doi: 10.1126/science.3529391. [DOI] [PubMed] [Google Scholar]
  207. Matsumura P., Rydel J. J., Linzmeier R., Vacante D. Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein. J Bacteriol. 1984 Oct;160(1):36–41. doi: 10.1128/jb.160.1.36-41.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  208. Matsuyama S., Mizuno T., Mizushima S. Interaction between two regulatory proteins in osmoregulatory expression of ompF and ompC genes in Escherichia coli: a novel ompR mutation suppresses pleiotropic defects caused by an envZ mutation. J Bacteriol. 1986 Dec;168(3):1309–1314. doi: 10.1128/jb.168.3.1309-1314.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  209. Matsuyama S., Mizushima S. Construction and characterization of a deletion mutant lacking micF, a proposed regulatory gene for OmpF synthesis in Escherichia coli. J Bacteriol. 1985 Jun;162(3):1196–1202. doi: 10.1128/jb.162.3.1196-1202.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  210. Matsuyama S., Mizushima S. Novel rpoA mutation that interferes with the function of OmpR and EnvZ, positive regulators of the ompF and ompC genes that code for outer-membrane proteins in Escherichia coli K12. J Mol Biol. 1987 Jun 20;195(4):847–853. doi: 10.1016/0022-2836(87)90489-x. [DOI] [PubMed] [Google Scholar]
  211. Mayer E. P., Smith O. H., Fredricks W. W., McKinney M. A. The isolation and characterization of glutamine-requiring strains of Escherichia coli K12. Mol Gen Genet. 1975;137(2):131–142. doi: 10.1007/BF00341679. [DOI] [PubMed] [Google Scholar]
  212. McBride M. J., Weinberg R. A., Zusman D. R. "Frizzy" aggregation genes of the gliding bacterium Myxococcus xanthus show sequence similarities to the chemotaxis genes of enteric bacteria. Proc Natl Acad Sci U S A. 1989 Jan;86(2):424–428. doi: 10.1073/pnas.86.2.424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  213. McClure W. R. Mechanism and control of transcription initiation in prokaryotes. Annu Rev Biochem. 1985;54:171–204. doi: 10.1146/annurev.bi.54.070185.001131. [DOI] [PubMed] [Google Scholar]
  214. McFarland N., McCarter L., Artz S., Kustu S. Nitrogen regulatory locus "glnR" of enteric bacteria is composed of cistrons ntrB and ntrC: identification of their protein products. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2135–2139. doi: 10.1073/pnas.78.4.2135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  215. McPherson M. J., Baron A. J., Pappin D. J., Wootton J. C. Respiratory nitrate reductase of Escherichia coli. Sequence identification of the large subunit gene. FEBS Lett. 1984 Nov 19;177(2):260–264. doi: 10.1016/0014-5793(84)81295-8. [DOI] [PubMed] [Google Scholar]
  216. Melchers L. S., Thompson D. V., Idler K. B., Schilperoort R. A., Hooykaas P. J. Nucleotide sequence of the virulence gene virG of the Agrobacterium tumefaciens octopine Ti plasmid: significant homology between virG and the regulatory genes ompR, phoB and dye of E. coli. Nucleic Acids Res. 1986 Dec 22;14(24):9933–9942. doi: 10.1093/nar/14.24.9933. [DOI] [PMC free article] [PubMed] [Google Scholar]
  217. Merrick M. J. Nitrogen control of the nif regulon in Klebsiella pneumoniae: involvement of the ntrA gene and analogies between ntrC and nifA. EMBO J. 1983;2(1):39–44. doi: 10.1002/j.1460-2075.1983.tb01377.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  218. Miller J. F., Mekalanos J. J., Falkow S. Coordinate regulation and sensory transduction in the control of bacterial virulence. Science. 1989 Feb 17;243(4893):916–922. doi: 10.1126/science.2537530. [DOI] [PubMed] [Google Scholar]
  219. Miller S. I., Kukral A. M., Mekalanos J. J. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc Natl Acad Sci U S A. 1989 Jul;86(13):5054–5058. doi: 10.1073/pnas.86.13.5054. [DOI] [PMC free article] [PubMed] [Google Scholar]
  220. Miller V. L., Taylor R. K., Mekalanos J. J. Cholera toxin transcriptional activator toxR is a transmembrane DNA binding protein. Cell. 1987 Jan 30;48(2):271–279. doi: 10.1016/0092-8674(87)90430-2. [DOI] [PubMed] [Google Scholar]
  221. Miranda-Ríos J., Sánchez-Pescador R., Urdea M., Covarrubias A. A. The complete nucleotide sequence of the glnALG operon of Escherichia coli K12. Nucleic Acids Res. 1987 Mar 25;15(6):2757–2770. doi: 10.1093/nar/15.6.2757. [DOI] [PMC free article] [PubMed] [Google Scholar]
  222. Mizuno T., Chou M. Y., Inouye M. A unique mechanism regulating gene expression: translational inhibition by a complementary RNA transcript (micRNA). Proc Natl Acad Sci U S A. 1984 Apr;81(7):1966–1970. doi: 10.1073/pnas.81.7.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  223. Mizuno T., Kato M., Jo Y. L., Mizushima S. Interaction of OmpR, a positive regulator, with the osmoregulated ompC and ompF genes of Escherichia coli. Studies with wild-type and mutant OmpR proteins. J Biol Chem. 1988 Jan 15;263(2):1008–1012. [PubMed] [Google Scholar]
  224. Mizuno T., Mizushima S. Characterization by deletion and localized mutagenesis in vitro of the promoter region of the Escherichia coli ompC gene and importance of the upstream DNA domain in positive regulation by the OmpR protein. J Bacteriol. 1986 Oct;168(1):86–95. doi: 10.1128/jb.168.1.86-95.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  225. Mizuno T., Wurtzel E. T., Inouye M. Osmoregulation of gene expression. II. DNA sequence of the envZ gene of the ompB operon of Escherichia coli and characterization of its gene product. J Biol Chem. 1982 Nov 25;257(22):13692–13698. [PubMed] [Google Scholar]
  226. Moolenaar G. F., van Sluis C. A., Backendorf C., van de Putte P. Regulation of the Escherichia coli excision repair gene uvrC. Overlap between the uvrC structural gene and the region coding for a 24 kD protein. Nucleic Acids Res. 1987 May 26;15(10):4273–4289. doi: 10.1093/nar/15.10.4273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  227. Mowbray S. L., Foster D. L., Koshland D. E., Jr Proteolytic fragments identified with domains of the aspartate chemoreceptor. J Biol Chem. 1985 Sep 25;260(21):11711–11718. [PubMed] [Google Scholar]
  228. Mullin D. A., Newton A. Ntr-like promoters and upstream regulatory sequence ftr are required for transcription of a developmentally regulated Caulobacter crescentus flagellar gene. J Bacteriol. 1989 Jun;171(6):3218–3227. doi: 10.1128/jb.171.6.3218-3227.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  229. Mullin D., Minnich S., Chen L. S., Newton A. A set of positively regulated flagellar gene promoters in Caulobacter crescentus with sequence homology to the nif gene promoters of Klebsiella pneumoniae. J Mol Biol. 1987 Jun 20;195(4):939–943. doi: 10.1016/0022-2836(87)90497-9. [DOI] [PubMed] [Google Scholar]
  230. Mutoh N., Simon M. I. Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli. J Bacteriol. 1986 Jan;165(1):161–166. doi: 10.1128/jb.165.1.161-166.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  231. Nagami Y., Tanaka T. Molecular cloning and nucleotide sequence of a DNA fragment from Bacillus natto that enhances production of extracellular proteases and levansucrase in Bacillus subtilis. J Bacteriol. 1986 Apr;166(1):20–28. doi: 10.1128/jb.166.1.20-28.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  232. Nara F., Matsuyama S., Mizuno T., Mizushima S. Molecular analysis of mutant ompR genes exhibiting different phenotypes as to osmoregulation of the ompF and ompC genes of Escherichia coli. Mol Gen Genet. 1986 Feb;202(2):194–199. doi: 10.1007/BF00331636. [DOI] [PubMed] [Google Scholar]
  233. Nelson S. O., Wright J. K., Postma P. W. The mechanism of inducer exclusion. Direct interaction between purified III of the phosphoenolpyruvate:sugar phosphotransferase system and the lactose carrier of Escherichia coli. EMBO J. 1983;2(5):715–720. doi: 10.1002/j.1460-2075.1983.tb01490.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  234. Newton A., Ohta N., Ramakrishnan G., Mullin D., Raymond G. Genetic switching in the flagellar gene hierarchy of Caulobacter requires negative as well as positive regulation of transcription. Proc Natl Acad Sci U S A. 1989 Sep;86(17):6651–6655. doi: 10.1073/pnas.86.17.6651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  235. Nikaido H., Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev. 1985 Mar;49(1):1–32. doi: 10.1128/mr.49.1.1-32.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  236. Ninfa A. J., Magasanik B. Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli. Proc Natl Acad Sci U S A. 1986 Aug;83(16):5909–5913. doi: 10.1073/pnas.83.16.5909. [DOI] [PMC free article] [PubMed] [Google Scholar]
  237. Ninfa A. J., Mullin D. A., Ramakrishnan G., Newton A. Escherichia coli sigma 54 RNA polymerase recognizes Caulobacter crescentus flbG and flaN flagellar gene promoters in vitro. J Bacteriol. 1989 Jan;171(1):383–391. doi: 10.1128/jb.171.1.383-391.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  238. Ninfa A. J., Ninfa E. G., Lupas A. N., Stock A., Magasanik B., Stock J. Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism. Proc Natl Acad Sci U S A. 1988 Aug;85(15):5492–5496. doi: 10.1073/pnas.85.15.5492. [DOI] [PMC free article] [PubMed] [Google Scholar]
  239. Ninfa A. J., Reitzer L. J., Magasanik B. Initiation of transcription at the bacterial glnAp2 promoter by purified E. coli components is facilitated by enhancers. Cell. 1987 Sep 25;50(7):1039–1046. doi: 10.1016/0092-8674(87)90170-x. [DOI] [PubMed] [Google Scholar]
  240. Ninfa A. J., Ueno-Nishio S., Hunt T. P., Robustell B., Magasanik B. Purification of nitrogen regulator II, the product of the glnL (ntrB) gene of Escherichia coli. J Bacteriol. 1986 Nov;168(2):1002–1004. doi: 10.1128/jb.168.2.1002-1004.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  241. Nishigaki I., Chen F. T., Hokin L. E. Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. XV. Direct chemical characterization of the acyl phosphate in the enzyme as an aspartyl beta-phosphate residue. J Biol Chem. 1974 Aug 10;249(15):4911–4916. [PubMed] [Google Scholar]
  242. Niwano M., Taylor B. L. Novel sensory adaptation mechanism in bacterial chemotaxis to oxygen and phosphotransferase substrates. Proc Natl Acad Sci U S A. 1982 Jan;79(1):11–15. doi: 10.1073/pnas.79.1.11. [DOI] [PMC free article] [PubMed] [Google Scholar]
  243. Nixon B. T., Ronson C. W., Ausubel F. M. Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7850–7854. doi: 10.1073/pnas.83.20.7850. [DOI] [PMC free article] [PubMed] [Google Scholar]
  244. Norioka S., Ramakrishnan G., Ikenaka K., Inouye M. Interaction of a transcriptional activator, OmpR, with reciprocally osmoregulated genes, ompF and ompC, of Escherichia coli. J Biol Chem. 1986 Dec 25;261(36):17113–17119. [PubMed] [Google Scholar]
  245. Oosawa K., Hess J. F., Simon M. I. Mutants defective in bacterial chemotaxis show modified protein phosphorylation. Cell. 1988 Apr 8;53(1):89–96. doi: 10.1016/0092-8674(88)90490-4. [DOI] [PubMed] [Google Scholar]
  246. Oosawa K., Mutoh N., Simon M. I. Cloning of the C-terminal cytoplasmic fragment of the tar protein and effects of the fragment on chemotaxis of Escherichia coli. J Bacteriol. 1988 Jun;170(6):2521–2526. doi: 10.1128/jb.170.6.2521-2526.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  247. Ostrow K. S., Silhavy T. J., Garrett S. cis-acting sites required for osmoregulation of ompF expression in Escherichia coli K-12. J Bacteriol. 1986 Dec;168(3):1165–1171. doi: 10.1128/jb.168.3.1165-1171.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  248. Osumi T., Saier M. H., Jr Regulation of lactose permease activity by the phosphoenolpyruvate:sugar phosphotransferase system: evidence for direct binding of the glucose-specific enzyme III to the lactose permease. Proc Natl Acad Sci U S A. 1982 Mar;79(5):1457–1461. doi: 10.1073/pnas.79.5.1457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  249. Overbeeke N., Bergmans H., van Mansfeld F., Lugtenberg B. Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12. J Mol Biol. 1983 Feb 5;163(4):513–532. doi: 10.1016/0022-2836(83)90110-9. [DOI] [PubMed] [Google Scholar]
  250. Ow D. W., Ausubel F. M. Regulation of nitrogen metabolism genes by nifA gene product in Klebsiella pneumoniae. Nature. 1983 Jan 27;301(5898):307–313. doi: 10.1038/301307a0. [DOI] [PubMed] [Google Scholar]
  251. Ow D. W., Sundaresan V., Rothstein D. M., Brown S. E., Ausubel F. M. Promoters regulated by the glnG (ntrC) and nifA gene products share a heptameric consensus sequence in the -15 region. Proc Natl Acad Sci U S A. 1983 May;80(9):2524–2528. doi: 10.1073/pnas.80.9.2524. [DOI] [PMC free article] [PubMed] [Google Scholar]
  252. Pahel G., Rothstein D. M., Magasanik B. Complex glnA-glnL-glnG operon of Escherichia coli. J Bacteriol. 1982 Apr;150(1):202–213. doi: 10.1128/jb.150.1.202-213.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  253. Pahel G., Tyler B. A new glnA-linked regulatory gene for glutamine synthetase in Escherichia coli. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4544–4548. doi: 10.1073/pnas.76.9.4544. [DOI] [PMC free article] [PubMed] [Google Scholar]
  254. Pahel G., Zelenetz A. D., Tyler B. M. gltB gene and regulation of nitrogen metabolism by glutamine synthetase in Escherichia coli. J Bacteriol. 1978 Jan;133(1):139–148. doi: 10.1128/jb.133.1.139-148.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  255. Parkinson J. S. Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis. J Bacteriol. 1978 Jul;135(1):45–53. doi: 10.1128/jb.135.1.45-53.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  256. Parkinson J. S., Houts S. E. Isolation and behavior of Escherichia coli deletion mutants lacking chemotaxis functions. J Bacteriol. 1982 Jul;151(1):106–113. doi: 10.1128/jb.151.1.106-113.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  257. Parkinson J. S., Parker S. R. Interaction of the cheC and cheZ gene products is required for chemotactic behavior in Escherichia coli. Proc Natl Acad Sci U S A. 1979 May;76(5):2390–2394. doi: 10.1073/pnas.76.5.2390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  258. Parkinson J. S., Parker S. R., Talbert P. B., Houts S. E. Interactions between chemotaxis genes and flagellar genes in Escherichia coli. J Bacteriol. 1983 Jul;155(1):265–274. doi: 10.1128/jb.155.1.265-274.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  259. Parkinson J. S., Revello P. T. Sensory adaptation mutants of E. coli. Cell. 1978 Dec;15(4):1221–1230. doi: 10.1016/0092-8674(78)90048-x. [DOI] [PubMed] [Google Scholar]
  260. Payne J. W., Gilvarg C. Size restriction on peptide utilization in Escherichia coli. J Biol Chem. 1968 Dec 10;243(23):6291–6299. [PubMed] [Google Scholar]
  261. Peng H. L., Novick R. P., Kreiswirth B., Kornblum J., Schlievert P. Cloning, characterization, and sequencing of an accessory gene regulator (agr) in Staphylococcus aureus. J Bacteriol. 1988 Sep;170(9):4365–4372. doi: 10.1128/jb.170.9.4365-4372.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  262. Pickart C. M., Jencks W. P. Energetics of the calcium-transporting ATPase. J Biol Chem. 1984 Feb 10;259(3):1629–1643. [PubMed] [Google Scholar]
  263. Pilkis S. J., Lively M. O., el-Maghrabi M. R. Active site sequence of hepatic fructose-2,6-bisphosphatase. Homology in primary structure with phosphoglycerate mutase. J Biol Chem. 1987 Sep 15;262(26):12672–12675. [PubMed] [Google Scholar]
  264. Popham D. L., Szeto D., Keener J., Kustu S. Function of a bacterial activator protein that binds to transcriptional enhancers. Science. 1989 Feb 3;243(4891):629–635. doi: 10.1126/science.2563595. [DOI] [PubMed] [Google Scholar]
  265. Post R. L., Kume S. Evidence for an aspartyl phosphate residue at the active site of sodium and potassium ion transport adenosine triphosphatase. J Biol Chem. 1973 Oct 25;248(20):6993–7000. [PubMed] [Google Scholar]
  266. Postma P. W., Lengeler J. W. Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria. Microbiol Rev. 1985 Sep;49(3):232–269. doi: 10.1128/mr.49.3.232-269.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  267. Prival M. J., Brenchley J. E., Magasanik B. Glutamine synthetase and the regulation of histidase formation in Klebsiella aerogenes. J Biol Chem. 1973 Jun 25;248(12):4334–4344. [PubMed] [Google Scholar]
  268. Ptashne M. Gene regulation by proteins acting nearby and at a distance. Nature. 1986 Aug 21;322(6081):697–701. doi: 10.1038/322697a0. [DOI] [PubMed] [Google Scholar]
  269. Ravid S., Eisenbach M. Direction of flagellar rotation in bacterial cell envelopes. J Bacteriol. 1984 Apr;158(1):222–230. doi: 10.1128/jb.158.1.222-230.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  270. Ravid S., Matsumura P., Eisenbach M. Restoration of flagellar clockwise rotation in bacterial envelopes by insertion of the chemotaxis protein CheY. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7157–7161. doi: 10.1073/pnas.83.19.7157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  271. Reitzer L. J., Bueno R., Cheng W. D., Abrams S. A., Rothstein D. M., Hunt T. P., Tyler B., Magasanik B. Mutations that create new promoters suppress the sigma 54 dependence of glnA transcription in Escherichia coli. J Bacteriol. 1987 Sep;169(9):4279–4284. doi: 10.1128/jb.169.9.4279-4284.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  272. Reitzer L. J., Magasanik B. Expression of glnA in Escherichia coli is regulated at tandem promoters. Proc Natl Acad Sci U S A. 1985 Apr;82(7):1979–1983. doi: 10.1073/pnas.82.7.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  273. Reitzer L. J., Magasanik B. Isolation of the nitrogen assimilation regulator NR(I), the product of the glnG gene of Escherichia coli. Proc Natl Acad Sci U S A. 1983 Sep;80(18):5554–5558. doi: 10.1073/pnas.80.18.5554. [DOI] [PMC free article] [PubMed] [Google Scholar]
  274. Reitzer L. J., Magasanik B. Transcription of glnA in E. coli is stimulated by activator bound to sites far from the promoter. Cell. 1986 Jun 20;45(6):785–792. doi: 10.1016/0092-8674(86)90553-2. [DOI] [PubMed] [Google Scholar]
  275. Reuveny Z., Foor F., Magasanik B. Regulation of glutamine synthetase by regulatory protein PII in Klebsiella aerogenes mutants lacking adenylyltransferase. J Bacteriol. 1981 May;146(2):740–745. doi: 10.1128/jb.146.2.740-745.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  276. Richardson J. S. The anatomy and taxonomy of protein structure. Adv Protein Chem. 1981;34:167–339. doi: 10.1016/s0065-3233(08)60520-3. [DOI] [PubMed] [Google Scholar]
  277. Riedel G. E., Brown S. E., Ausubel F. M. Nitrogen fixation by Klebsiella pneumoniae is inhibited by certain multicopy hybrid nif plasmids. J Bacteriol. 1983 Jan;153(1):45–56. doi: 10.1128/jb.153.1.45-56.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  278. Robertson E. F., Hoyt J. C., Reeves H. C. Evidence of histidine phosphorylation in isocitrate lyase from Escherichia coli. J Biol Chem. 1988 Feb 15;263(5):2477–2482. [PubMed] [Google Scholar]
  279. Ronson C. W., Astwood P. M., Downie J. A. Molecular cloning and genetic organization of C4-dicarboxylate transport genes from Rhizobium leguminosarum. J Bacteriol. 1984 Dec;160(3):903–909. doi: 10.1128/jb.160.3.903-909.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  280. Ronson C. W., Astwood P. M., Nixon B. T., Ausubel F. M. Deduced products of C4-dicarboxylate transport regulatory genes of Rhizobium leguminosarum are homologous to nitrogen regulatory gene products. Nucleic Acids Res. 1987 Oct 12;15(19):7921–7934. doi: 10.1093/nar/15.19.7921. [DOI] [PMC free article] [PubMed] [Google Scholar]
  281. Ronson C. W., Nixon B. T., Albright L. M., Ausubel F. M. Rhizobium meliloti ntrA (rpoN) gene is required for diverse metabolic functions. J Bacteriol. 1987 Jun;169(6):2424–2431. doi: 10.1128/jb.169.6.2424-2431.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  282. Ronson C. W., Nixon B. T., Ausubel F. M. Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell. 1987 Jun 5;49(5):579–581. doi: 10.1016/0092-8674(87)90530-7. [DOI] [PubMed] [Google Scholar]
  283. Rose Z. B. Intermediates in the phosphoglycerate mutase and bisphosphoglycerate synthase reactions. Methods Enzymol. 1982;87:42–51. doi: 10.1016/s0076-6879(82)87006-7. [DOI] [PubMed] [Google Scholar]
  284. Rosenberg H., Gerdes R. G., Chegwidden K. Two systems for the uptake of phosphate in Escherichia coli. J Bacteriol. 1977 Aug;131(2):505–511. doi: 10.1128/jb.131.2.505-511.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  285. Rubik B. A., Koshland D. E., Jr Potentiation, desensitization, and inversion of response in bacterial sensing of chemical stimuli. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2820–2824. doi: 10.1073/pnas.75.6.2820. [DOI] [PMC free article] [PubMed] [Google Scholar]
  286. Saier M. H., Jr Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Microbiol Rev. 1989 Mar;53(1):109–120. doi: 10.1128/mr.53.1.109-120.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  287. Saier M. H., Jr, Wentzel D. L., Feucht B. U., Judice J. J. A transport system for phosphoenolpyruvate, 2-phosphoglycerate, and 3-phosphoglycerate in Salmonella typhimurium. J Biol Chem. 1975 Jul 10;250(13):5089–5096. [PubMed] [Google Scholar]
  288. Saier M. H., Jr, Yamada M., Erni B., Suda K., Lengeler J., Ebner R., Argos P., Rak B., Schnetz K., Lee C. A. Sugar permeases of the bacterial phosphoenolpyruvate-dependent phosphotransferase system: sequence comparisons. FASEB J. 1988 Mar 1;2(3):199–208. doi: 10.1096/fasebj.2.3.2832233. [DOI] [PubMed] [Google Scholar]
  289. Sanders D. A., Koshland D. E., Jr Receptor interactions through phosphorylation and methylation pathways in bacterial chemotaxis. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8425–8429. doi: 10.1073/pnas.85.22.8425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  290. Sarma V., Reeves P. Genetic locus (ompB) affecting a major outer-membrane protein in Escherichia coli K-12. J Bacteriol. 1977 Oct;132(1):23–27. doi: 10.1128/jb.132.1.23-27.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  291. Sasse-Dwight S., Gralla J. D. Probing the Escherichia coli glnALG upstream activation mechanism in vivo. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8934–8938. doi: 10.1073/pnas.85.23.8934. [DOI] [PMC free article] [PubMed] [Google Scholar]
  292. Sato T., Yura T. Chromosomal location and expression of the structural gene for major outer membrane protein Ia of Escherichia coli K-12 and of the homologous gene of Salmonella typhimurium. J Bacteriol. 1979 Aug;139(2):468–477. doi: 10.1128/jb.139.2.468-477.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  293. Schnaitman C. A., McDonald G. A. Regulation of outer membrane protein synthesis in Escherichia coli K-12: deletion of ompC affects expression of the OmpF protein. J Bacteriol. 1984 Aug;159(2):555–563. doi: 10.1128/jb.159.2.555-563.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  294. Schnaitman C. A. Outer membrane proteins of Escherichia coli. IV. Differences in outer membrane proteins due to strain and cultural differences. J Bacteriol. 1974 May;118(2):454–464. doi: 10.1128/jb.118.2.454-464.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  295. Schweizer H., Boos W. Cloning of the ugp region containing the structural genes for the pho regulon-dependent sn-glycerol-3-phosphate transport system of Escherichia coli. Mol Gen Genet. 1983;192(1-2):177–186. doi: 10.1007/BF00327664. [DOI] [PubMed] [Google Scholar]
  296. Segall J. E., Ishihara A., Berg H. C. Chemotactic signaling in filamentous cells of Escherichia coli. J Bacteriol. 1985 Jan;161(1):51–59. doi: 10.1128/jb.161.1.51-59.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  297. Segall J. E., Manson M. D., Berg H. C. Signal processing times in bacterial chemotaxis. Nature. 1982 Apr 29;296(5860):855–857. doi: 10.1038/296855a0. [DOI] [PubMed] [Google Scholar]
  298. Seki T., Yoshikawa H., Takahashi H., Saito H. Cloning and nucleotide sequence of phoP, the regulatory gene for alkaline phosphatase and phosphodiesterase in Bacillus subtilis. J Bacteriol. 1987 Jul;169(7):2913–2916. doi: 10.1128/jb.169.7.2913-2916.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  299. Seki T., Yoshikawa H., Takahashi H., Saito H. Nucleotide sequence of the Bacillus subtilis phoR gene. J Bacteriol. 1988 Dec;170(12):5935–5938. doi: 10.1128/jb.170.12.5935-5938.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  300. Serrano R., Kielland-Brandt M. C., Fink G. R. Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases. Nature. 1986 Feb 20;319(6055):689–693. doi: 10.1038/319689a0. [DOI] [PubMed] [Google Scholar]
  301. Sharma S., Stark T. F., Beattie W. G., Moses R. E. Multiple control elements for the uvrC gene unit of Escherichia coli. Nucleic Acids Res. 1986 Mar 11;14(5):2301–2318. doi: 10.1093/nar/14.5.2301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  302. Shaw D. J., Rice D. W., Guest J. R. Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli. J Mol Biol. 1983 May 15;166(2):241–247. doi: 10.1016/s0022-2836(83)80011-4. [DOI] [PubMed] [Google Scholar]
  303. Shimotsu H., Henner D. J. Modulation of Bacillus subtilis levansucrase gene expression by sucrose and regulation of the steady-state mRNA level by sacU and sacQ genes. J Bacteriol. 1986 Oct;168(1):380–388. doi: 10.1128/jb.168.1.380-388.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  304. Shinagawa H., Makino K., Nakata A. Regulation of the pho regulon in Escherichia coli K-12. Genetic and physiological regulation of the positive regulatory gene phoB. J Mol Biol. 1983 Aug 15;168(3):477–488. doi: 10.1016/s0022-2836(83)80297-6. [DOI] [PubMed] [Google Scholar]
  305. Shioi J. I., Galloway R. J., Niwano M., Chinnock R. E., Taylor B. L. Requirement of ATP in bacterial chemotaxis. J Biol Chem. 1982 Jul 25;257(14):7969–7975. [PubMed] [Google Scholar]
  306. Shioi J., Tribhuwan R. C., Berg S. T., Taylor B. L. Signal transduction in chemotaxis to oxygen in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1988 Dec;170(12):5507–5511. doi: 10.1128/jb.170.12.5507-5511.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  307. Shoji K., Hiratsuka S., Kawamura F., Kobayashi Y. New suppressor mutation sur0B of spo0B and spo0F mutations in Bacillus subtilis. J Gen Microbiol. 1988 Dec;134(12):3249–3257. doi: 10.1099/00221287-134-12-3249. [DOI] [PubMed] [Google Scholar]
  308. Shull G. E., Lingrel J. B. Molecular cloning of the rat stomach (H+ + K+)-ATPase. J Biol Chem. 1986 Dec 25;261(36):16788–16791. [PubMed] [Google Scholar]
  309. Shull G. E., Schwartz A., Lingrel J. B. Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA. Nature. 1985 Aug 22;316(6030):691–695. doi: 10.1038/316691a0. [DOI] [PubMed] [Google Scholar]
  310. Silverman M., Simon M. Identification of polypeptides necessary for chemotaxis in Escherichia coli. J Bacteriol. 1977 Jun;130(3):1317–1325. doi: 10.1128/jb.130.3.1317-1325.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  311. Simms S. A., Keane M. G., Stock J. Multiple forms of the CheB methylesterase in bacterial chemosensing. J Biol Chem. 1985 Aug 25;260(18):10161–10168. [PubMed] [Google Scholar]
  312. Simms S. A., Stock A. M., Stock J. B. Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria. J Biol Chem. 1987 Jun 25;262(18):8537–8543. [PubMed] [Google Scholar]
  313. Slauch J. M., Garrett S., Jackson D. E., Silhavy T. J. EnvZ functions through OmpR to control porin gene expression in Escherichia coli K-12. J Bacteriol. 1988 Jan;170(1):439–441. doi: 10.1128/jb.170.1.439-441.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  314. Smith J. M., Rowsell E. H., Shioi J., Taylor B. L. Identification of a site of ATP requirement for signal processing in bacterial chemotaxis. J Bacteriol. 1988 Jun;170(6):2698–2704. doi: 10.1128/jb.170.6.2698-2704.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  315. Smith R. A., Parkinson J. S. Overlapping genes at the cheA locus of Escherichia coli. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5370–5374. doi: 10.1073/pnas.77.9.5370. [DOI] [PMC free article] [PubMed] [Google Scholar]
  316. Sodergren E. J., DeMoss J. A. narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes. J Bacteriol. 1988 Apr;170(4):1721–1729. doi: 10.1128/jb.170.4.1721-1729.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  317. Springer M. S., Goy M. F., Adler J. Protein methylation in behavioural control mechanisms and in signal transduction. Nature. 1979 Jul 26;280(5720):279–284. doi: 10.1038/280279a0. [DOI] [PubMed] [Google Scholar]
  318. Springer M. S., Goy M. F., Adler J. Sensory transduction in Escherichia coli: two complementary pathways of information processing that involve methylated proteins. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3312–3316. doi: 10.1073/pnas.74.8.3312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  319. Springer M. S., Zanolari B., Pierzchala P. A. Ordered methylation of the methyl-accepting chemotaxis proteins of Escherichia coli. J Biol Chem. 1982 Jun 25;257(12):6861–6866. [PubMed] [Google Scholar]
  320. Springer M. S., Zanolari B. Sensory transduction in Escherichia coli: regulation of the demethylation rate by the CheA protein. Proc Natl Acad Sci U S A. 1984 Aug;81(16):5061–5065. doi: 10.1073/pnas.81.16.5061. [DOI] [PMC free article] [PubMed] [Google Scholar]
  321. Springer W. R., Koshland D. E., Jr Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system. Proc Natl Acad Sci U S A. 1977 Feb;74(2):533–537. doi: 10.1073/pnas.74.2.533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  322. Spronk A. M., Yoshida H., Wood H. G. Isolation of 3-phosphohistidine from phosphorylated pyruvate, phosphate dikinase. Proc Natl Acad Sci U S A. 1976 Dec;73(12):4415–4419. doi: 10.1073/pnas.73.12.4415. [DOI] [PMC free article] [PubMed] [Google Scholar]
  323. Stachel S. E., Nester E. W. The genetic and transcriptional organization of the vir region of the A6 Ti plasmid of Agrobacterium tumefaciens. EMBO J. 1986 Jul;5(7):1445–1454. doi: 10.1002/j.1460-2075.1986.tb04381.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  324. Stachel S. E., Zambryski P. C. virA and virG control the plant-induced activation of the T-DNA transfer process of A. tumefaciens. Cell. 1986 Aug 1;46(3):325–333. doi: 10.1016/0092-8674(86)90653-7. [DOI] [PubMed] [Google Scholar]
  325. Stadtman E. R., Chock P. B. Interconvertible enzyme cascades in metabolic regulation. Curr Top Cell Regul. 1978;13:53–95. doi: 10.1016/b978-0-12-152813-3.50007-0. [DOI] [PubMed] [Google Scholar]
  326. Stelte B., Witzel H. Formation of an aspartyl phosphate intermediate in the reactions of nucleoside phosphotransferase from carrots. Eur J Biochem. 1986 Feb 17;155(1):121–124. doi: 10.1111/j.1432-1033.1986.tb09466.x. [DOI] [PubMed] [Google Scholar]
  327. Stewart R. C., Dahlquist F. W. N-terminal half of CheB is involved in methylesterase response to negative chemotactic stimuli in Escherichia coli. J Bacteriol. 1988 Dec;170(12):5728–5738. doi: 10.1128/jb.170.12.5728-5738.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  328. Stewart V. Nitrate respiration in relation to facultative metabolism in enterobacteria. Microbiol Rev. 1988 Jun;52(2):190–232. doi: 10.1128/mr.52.2.190-232.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  329. Stewart V., Parales J., Jr Identification and expression of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12. J Bacteriol. 1988 Apr;170(4):1589–1597. doi: 10.1128/jb.170.4.1589-1597.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  330. Stewart V., Parales J., Jr, Merkel S. M. Structure of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12. J Bacteriol. 1989 Apr;171(4):2229–2234. doi: 10.1128/jb.171.4.2229-2234.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  331. Stibitz S., Aaronson W., Monack D., Falkow S. Phase variation in Bordetella pertussis by frameshift mutation in a gene for a novel two-component system. Nature. 1989 Mar 16;338(6212):266–269. doi: 10.1038/338266a0. [DOI] [PubMed] [Google Scholar]
  332. Stock A. M., Mottonen J. M., Stock J. B., Schutt C. E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature. 1989 Feb 23;337(6209):745–749. doi: 10.1038/337745a0. [DOI] [PubMed] [Google Scholar]
  333. Stock A. M., Stock J. B. Purification and characterization of the CheZ protein of bacterial chemotaxis. J Bacteriol. 1987 Jul;169(7):3301–3311. doi: 10.1128/jb.169.7.3301-3311.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  334. Stock A. M., Wylie D. C., Mottonen J. M., Lupas A. N., Ninfa E. G., Ninfa A. J., Schutt C. E., Stock J. B. Phosphoproteins involved in bacterial signal transduction. Cold Spring Harb Symp Quant Biol. 1988;53(Pt 1):49–57. doi: 10.1101/sqb.1988.053.01.009. [DOI] [PubMed] [Google Scholar]
  335. Stock A., Chen T., Welsh D., Stock J. CheA protein, a central regulator of bacterial chemotaxis, belongs to a family of proteins that control gene expression in response to changing environmental conditions. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1403–1407. doi: 10.1073/pnas.85.5.1403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  336. Stock A., Koshland D. E., Jr, Stock J. Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation. Proc Natl Acad Sci U S A. 1985 Dec;82(23):7989–7993. doi: 10.1073/pnas.82.23.7989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  337. Stock A., Mottonen J., Chen T., Stock J. Identification of a possible nucleotide binding site in CheW, a protein required for sensory transduction in bacterial chemotaxis. J Biol Chem. 1987 Jan 15;262(2):535–537. [PubMed] [Google Scholar]
  338. Stock J. B., Koshland D. E., Jr Changing reactivity of receptor carboxyl groups during bacterial sensing. J Biol Chem. 1981 Nov 10;256(21):10826–10833. [PubMed] [Google Scholar]
  339. Stock J. B., Maderis A. M., Koshland D. E., Jr Bacterial chemotaxis in the absence of receptor carboxylmethylation. Cell. 1981 Nov;27(1 Pt 2):37–44. doi: 10.1016/0092-8674(81)90358-5. [DOI] [PubMed] [Google Scholar]
  340. Stock J. B., Rauch B., Roseman S. Periplasmic space in Salmonella typhimurium and Escherichia coli. J Biol Chem. 1977 Nov 10;252(21):7850–7861. [PubMed] [Google Scholar]
  341. Stock J., Borczuk A., Chiou F., Burchenal J. E. Compensatory mutations in receptor function: a reevaluation of the role of methylation in bacterial chemotaxis. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8364–8368. doi: 10.1073/pnas.82.24.8364. [DOI] [PMC free article] [PubMed] [Google Scholar]
  342. Stock J., Kersulis G., Koshland D. E., Jr Neither methylating nor demethylating enzymes are required for bacterial chemotaxis. Cell. 1985 Sep;42(2):683–690. doi: 10.1016/0092-8674(85)90125-4. [DOI] [PubMed] [Google Scholar]
  343. Stock J. Mechanisms of receptor function and the molecular biology of information processing in bacteria. Bioessays. 1987 May;6(5):199–203. doi: 10.1002/bies.950060502. [DOI] [PubMed] [Google Scholar]
  344. Stock J., Simms S. Methylation, demethylation, and deamidation at glutamate residues in membrane chemoreceptor proteins. Adv Exp Med Biol. 1988;231:201–212. doi: 10.1007/978-1-4684-9042-8_16. [DOI] [PubMed] [Google Scholar]
  345. Stoker K., Reijnders W. N., Oltmann L. F., Stouthamer A. H. Initial cloning and sequencing of hydHG, an operon homologous to ntrBC and regulating the labile hydrogenase activity in Escherichia coli K-12. J Bacteriol. 1989 Aug;171(8):4448–4456. doi: 10.1128/jb.171.8.4448-4456.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  346. Sundaresan V., Ow D. W., Ausubel F. M. Activation of Klebsiella pneumoniae and Rhizobium meliloti nitrogenase promoters by gln (ntr) regulatory proteins. Proc Natl Acad Sci U S A. 1983 Jul;80(13):4030–4034. doi: 10.1073/pnas.80.13.4030. [DOI] [PMC free article] [PubMed] [Google Scholar]
  347. Surin B. P., Dixon N. E., Rosenberg H. Purification of the phoU protein, a negative regulator of the pho regulon of Escherichia coli K-12. J Bacteriol. 1986 Nov;168(2):631–635. doi: 10.1128/jb.168.2.631-635.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  348. Surin B. P., Jans D. A., Fimmel A. L., Shaw D. C., Cox G. B., Rosenberg H. Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene. J Bacteriol. 1984 Mar;157(3):772–778. doi: 10.1128/jb.157.3.772-778.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  349. Surin B. P., Rosenberg H., Cox G. B. Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships. J Bacteriol. 1985 Jan;161(1):189–198. doi: 10.1128/jb.161.1.189-198.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  350. Szeto W. W., Nixon B. T., Ronson C. W., Ausubel F. M. Identification and characterization of the Rhizobium meliloti ntrC gene: R. meliloti has separate regulatory pathways for activation of nitrogen fixation genes in free-living and symbiotic cells. J Bacteriol. 1987 Apr;169(4):1423–1432. doi: 10.1128/jb.169.4.1423-1432.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  351. TORRIANI A. Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli. Biochim Biophys Acta. 1960 Mar 11;38:460–469. doi: 10.1016/0006-3002(60)91281-6. [DOI] [PubMed] [Google Scholar]
  352. TORRIANI A., ROTHMAN F. Mutants of Escherichia coli constitutive for alkaline phosphatase. J Bacteriol. 1961 May;81:835–836. doi: 10.1128/jb.81.5.835-836.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  353. Tanaka T., Kawata M. Cloning and characterization of Bacillus subtilis iep, which has positive and negative effects on production of extracellular proteases. J Bacteriol. 1988 Aug;170(8):3593–3600. doi: 10.1128/jb.170.8.3593-3600.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  354. Tanaka T., Kawata M., Nagami Y., Uchiyama H. prtR enhances the mRNA level of the Bacillus subtilis extracellular proteases. J Bacteriol. 1987 Jul;169(7):3044–3050. doi: 10.1128/jb.169.7.3044-3050.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  355. Tanford C. Twenty questions concerning the reaction cycle of the sarcoplasmic reticulum calcium pump. CRC Crit Rev Biochem. 1984;17(2):123–151. doi: 10.3109/10409238409113603. [DOI] [PubMed] [Google Scholar]
  356. Tate S., Kato M., Nishimura Y., Arata Y., Mizuno T. Location of DNA-binding segment of a positive regulator, OmpR, involved in activation of the ompF and ompC genes of Escherichia coli. FEBS Lett. 1988 Dec 19;242(1):27–30. doi: 10.1016/0014-5793(88)80978-5. [DOI] [PubMed] [Google Scholar]
  357. Taylor R. K., Garrett S., Sodergren E., Silhavy T. J. Mutations that define the promoter of ompF, a gene specifying a major outer membrane porin protein. J Bacteriol. 1985 Jun;162(3):1054–1060. doi: 10.1128/jb.162.3.1054-1060.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  358. Terwilliger T. C., Koshland D. E., Jr Sites of methyl esterification and deamination on the aspartate receptor involved in chemotaxis. J Biol Chem. 1984 Jun 25;259(12):7719–7725. [PubMed] [Google Scholar]
  359. Tommassen J., Heimstra P., Overduin P., Lugtenberg B. Cloning of phoM, a gene involved in regulation of the synthesis of phosphate limitation inducible proteins in Escherichia coli K12. Mol Gen Genet. 1984;195(1-2):190–194. doi: 10.1007/BF00332745. [DOI] [PubMed] [Google Scholar]
  360. Tommassen J., de Geus P., Lugtenberg B., Hackett J., Reeves P. Regulation of the pho regulon of Escherichia coli K-12. Cloning of the regulatory genes phoB and phoR and identification of their gene products. J Mol Biol. 1982 May 15;157(2):265–274. doi: 10.1016/0022-2836(82)90233-9. [DOI] [PubMed] [Google Scholar]
  361. Trach K. A., Chapman J. W., Piggot P. J., Hoch J. A. Deduced product of the stage 0 sporulation gene spo0F shares homology with the Spo0A, OmpR, and SfrA proteins. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7260–7264. doi: 10.1073/pnas.82.21.7260. [DOI] [PMC free article] [PubMed] [Google Scholar]
  362. Trach K., Chapman J. W., Piggot P., LeCoq D., Hoch J. A. Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome. J Bacteriol. 1988 Sep;170(9):4194–4208. doi: 10.1128/jb.170.9.4194-4208.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  363. Tyler B. Regulation of the assimilation of nitrogen compounds. Annu Rev Biochem. 1978;47:1127–1162. doi: 10.1146/annurev.bi.47.070178.005403. [DOI] [PubMed] [Google Scholar]
  364. Ueno-Nishio S., Mango S., Reitzer L. J., Magasanik B. Identification and regulation of the glnL operator-promoter of the complex glnALG operon of Escherichia coli. J Bacteriol. 1984 Oct;160(1):379–384. doi: 10.1128/jb.160.1.379-384.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  365. Veech R. L., Lawson J. W., Cornell N. W., Krebs H. A. Cytosolic phosphorylation potential. J Biol Chem. 1979 Jul 25;254(14):6538–6547. [PubMed] [Google Scholar]
  366. Verhoef C., Lugtenberg B., van Boxtel R., de Graaff P., Verheij H. Genetics and biochemistry of the peptidoglycan-associated proteins b and c of Escherichia coli K12. Mol Gen Genet. 1979 Jan 31;169(2):137–146. doi: 10.1007/BF00271664. [DOI] [PubMed] [Google Scholar]
  367. Verhoef C., de Graaff P. J., Lugtenberg E. J. Mapping of a gene for a major outer membrane protein of Escherichia coli K12 with the aid of a newly isolated bacteriophage. Mol Gen Genet. 1977 Jan 7;150(1):103–105. doi: 10.1007/BF02425330. [DOI] [PubMed] [Google Scholar]
  368. Villarejo M., Case C. C. envZ mediates transcriptional control by local anesthetics but is not required for osmoregulation in Escherichia coli. J Bacteriol. 1984 Sep;159(3):883–887. doi: 10.1128/jb.159.3.883-887.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  369. Wandersman C., Moreno F., Schwartz M. Pleiotropic mutations rendering Escherichia coli K-12 resistant to bacteriophage TP1. J Bacteriol. 1980 Sep;143(3):1374–1383. doi: 10.1128/jb.143.3.1374-1383.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  370. Wang E. A., Koshland D. E., Jr Receptor structure in the bacterial sensing system. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7157–7161. doi: 10.1073/pnas.77.12.7157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  371. Wang T., Jurásek L., Bridger W. A. Succinyl coenzyme A synthetase of Escherichia coli. Sequence of a peptide containing the active-site phosphohistidine residue. Biochemistry. 1972 May 23;11(11):2067–2070. doi: 10.1021/bi00761a011. [DOI] [PubMed] [Google Scholar]
  372. Wanner B. L. Bacterial alkaline phosphatase clonal variation in some Escherichia coli K-12 phoR mutant strains. J Bacteriol. 1986 Dec;168(3):1366–1371. doi: 10.1128/jb.168.3.1366-1371.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  373. Wanner B. L., Latterell P. Mutants affected in alkaline phosphatase, expression: evidence for multiple positive regulators of the phosphate regulon in Escherichia coli. Genetics. 1980 Oct;96(2):353–366. doi: 10.1093/genetics/96.2.353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  374. Wanner B. L., McSharry R. Phosphate-controlled gene expression in Escherichia coli K12 using Mudl-directed lacZ fusions. J Mol Biol. 1982 Jul 5;158(3):347–363. doi: 10.1016/0022-2836(82)90202-9. [DOI] [PubMed] [Google Scholar]
  375. Wanner B. L. Overlapping and separate controls on the phosphate regulon in Escherichia coli K12. J Mol Biol. 1983 May 25;166(3):283–308. doi: 10.1016/s0022-2836(83)80086-2. [DOI] [PubMed] [Google Scholar]
  376. Wanner B. L., Sarthy A., Beckwith J. Escherichia coli pleiotropic mutant that reduces amounts of several periplasmic and outer membrane proteins. J Bacteriol. 1979 Oct;140(1):229–239. doi: 10.1128/jb.140.1.229-239.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  377. Wanner B. L., Wilmes M. R., Young D. C. Control of bacterial alkaline phosphatase synthesis and variation in an Escherichia coli K-12 phoR mutant by adenyl cyclase, the cyclic AMP receptor protein, and the phoM operon. J Bacteriol. 1988 Mar;170(3):1092–1102. doi: 10.1128/jb.170.3.1092-1102.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  378. Warrick H. M., Taylor B. L., Koshland D. E., Jr Chemotactic mechanism of Salmonella typhimurium: preliminary mapping and characterization of mutants. J Bacteriol. 1977 Apr;130(1):223–231. doi: 10.1128/jb.130.1.223-231.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  379. Weber R. F., Silverman P. M. The cpx proteins of Escherichia coli K12. Structure of the cpxA polypeptide as an inner membrane component. J Mol Biol. 1988 Sep 20;203(2):467–478. doi: 10.1016/0022-2836(88)90013-7. [DOI] [PubMed] [Google Scholar]
  380. Weglenski P., Ninfa A. J., Ueno-Nishio S., Magasanik B. Mutations in the glnG gene of Escherichia coli that result in increased activity of nitrogen regulator I. J Bacteriol. 1989 Aug;171(8):4479–4485. doi: 10.1128/jb.171.8.4479-4485.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  381. Weigel N., Kukuruzinska M. A., Nakazawa A., Waygood E. B., Roseman S. Sugar transport by the bacterial phosphotransferase system. Phosphoryl transfer reactions catalyzed by enzyme I of Salmonella typhimurium. J Biol Chem. 1982 Dec 10;257(23):14477–14491. [PubMed] [Google Scholar]
  382. Weiss V., Magasanik B. Phosphorylation of nitrogen regulator I (NRI) of Escherichia coli. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8919–8923. doi: 10.1073/pnas.85.23.8919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  383. Weston L. A., Kadner R. J. Identification of uhp polypeptides and evidence for their role in exogenous induction of the sugar phosphate transport system of Escherichia coli K-12. J Bacteriol. 1987 Aug;169(8):3546–3555. doi: 10.1128/jb.169.8.3546-3555.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  384. Weston L. A., Kadner R. J. Role of uhp genes in expression of the Escherichia coli sugar-phosphate transport system. J Bacteriol. 1988 Aug;170(8):3375–3383. doi: 10.1128/jb.170.8.3375-3383.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  385. Widenhorn K. A., Boos W., Somers J. M., Kay W. W. Cloning and properties of the Salmonella typhimurium tricarboxylate transport operon in Escherichia coli. J Bacteriol. 1988 Feb;170(2):883–888. doi: 10.1128/jb.170.2.883-888.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  386. Williams S. P., Sykes B. D., Bridger W. A. Phosphorus-31 nuclear magnetic resonance study of the active site phosphohistidine and regulatory phosphoserine residues of rat liver ATP-citrate lyase. Biochemistry. 1985 Sep 24;24(20):5527–5531. doi: 10.1021/bi00341a037. [DOI] [PubMed] [Google Scholar]
  387. Winans S. C., Ebert P. R., Stachel S. E., Gordon M. P., Nester E. W. A gene essential for Agrobacterium virulence is homologous to a family of positive regulatory loci. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8278–8282. doi: 10.1073/pnas.83.21.8278. [DOI] [PMC free article] [PubMed] [Google Scholar]
  388. Winans S. C., Kerstetter R. A., Nester E. W. Transcriptional regulation of the virA and virG genes of Agrobacterium tumefaciens. J Bacteriol. 1988 Sep;170(9):4047–4054. doi: 10.1128/jb.170.9.4047-4054.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  389. Winkler H. H. Compartmentation in the induction of the hexose-6-phosphate transport system of Escherichia coli. J Bacteriol. 1970 Feb;101(2):470–475. doi: 10.1128/jb.101.2.470-475.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  390. Wolfe A. J., Conley M. P., Berg H. C. Acetyladenylate plays a role in controlling the direction of flagellar rotation. Proc Natl Acad Sci U S A. 1988 Sep;85(18):6711–6715. doi: 10.1073/pnas.85.18.6711. [DOI] [PMC free article] [PubMed] [Google Scholar]
  391. Wolfe A. J., Conley M. P., Kramer T. J., Berg H. C. Reconstitution of signaling in bacterial chemotaxis. J Bacteriol. 1987 May;169(5):1878–1885. doi: 10.1128/jb.169.5.1878-1885.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  392. Wong P. K., Popham D., Keener J., Kustu S. In vitro transcription of the nitrogen fixation regulatory operon nifLA of Klebsiella pneumoniae. J Bacteriol. 1987 Jun;169(6):2876–2880. doi: 10.1128/jb.169.6.2876-2880.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  393. Wylie D., Stock A., Wong C. Y., Stock J. Sensory transduction in bacterial chemotaxis involves phosphotransfer between Che proteins. Biochem Biophys Res Commun. 1988 Mar 15;151(2):891–896. doi: 10.1016/s0006-291x(88)80365-6. [DOI] [PubMed] [Google Scholar]
  394. Yamaguchi S., Aizawa S., Kihara M., Isomura M., Jones C. J., Macnab R. M. Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium. J Bacteriol. 1986 Dec;168(3):1172–1179. doi: 10.1128/jb.168.3.1172-1179.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  395. Yamaguchi S., Fujita H., Ishihara A., Aizawa S., Macnab R. M. Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching. J Bacteriol. 1986 Apr;166(1):187–193. doi: 10.1128/jb.166.1.187-193.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  396. Yang M., Ferrari E., Chen E., Henner D. J. Identification of the pleiotropic sacQ gene of Bacillus subtilis. J Bacteriol. 1986 Apr;166(1):113–119. doi: 10.1128/jb.166.1.113-119.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  397. Yang Y. L., Goldrick D., Hong J. S. Identification of the products and nucleotide sequences of two regulatory genes involved in the exogenous induction of phosphoglycerate transport in Salmonella typhimurium. J Bacteriol. 1988 Sep;170(9):4299–4303. doi: 10.1128/jb.170.9.4299-4303.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  398. Yonekawa H., Hayashi H., Parkinson J. S. Requirement of the cheB function for sensory adaptation in Escherichia coli. J Bacteriol. 1983 Dec;156(3):1228–1235. doi: 10.1128/jb.156.3.1228-1235.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  399. Yu G. Q., Hong J. S. Identification and nucleotide sequence of the activator gene of the externally induced phosphoglycerate transport system of Salmonella typhimurium. Gene. 1986;45(1):51–57. doi: 10.1016/0378-1119(86)90131-9. [DOI] [PubMed] [Google Scholar]
  400. Zusman D. R. "Frizzy" mutants: a new class of aggregation-defective developmental mutants of Myxococcus xanthus. J Bacteriol. 1982 Jun;150(3):1430–1437. doi: 10.1128/jb.150.3.1430-1437.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  401. van Alphen L., Lugtenberg B., van Boxtel R., Hack A. M., Verhoef C., Havekes L. meoA is the structural gene for outer membrane protein c of Escherichia coli K12. Mol Gen Genet. 1979 Jan 31;169(2):147–155. doi: 10.1007/BF00271665. [DOI] [PubMed] [Google Scholar]

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