Skip to main content
PMC home page
Microbiological Reviews logoLink to Microbiological Reviews
. 1993 Jun;57(2):320–346. doi: 10.1128/mr.57.2.320-346.1993

Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria.

R Tam 1, M H Saier Jr 1
PMCID: PMC372912  PMID: 8336670

Abstract

Extracellular solute-binding proteins of bacteria serve as chemoreceptors, recognition constituents of transport systems, and initiators of signal transduction pathways. Over 50 sequenced periplasmic solute-binding proteins of gram-negative bacteria and homologous extracytoplasmic lipoproteins of gram-positive bacteria have been analyzed for sequence similarities, and their degrees of relatedness have been determined. Some of these proteins are homologous to cytoplasmic transcriptional regulatory proteins of bacteria; however, with the sole exception of the vitamin B12-binding protein of Escherichia coli, which is homologous to human glutathione peroxidase, they are not demonstrably homologous to any of the several thousand sequenced eukaryotic proteins. Most of these proteins fall into eight distinct clusters as follows. Cluster 1 solute-binding proteins are specific for malto-oligosaccharides, multiple oligosaccharides, glycerol 3-phosphate, and iron. Cluster 2 proteins are specific for galactose, ribose, arabinose, and multiple monosaccharides, and they are homologous to a number of transcriptional regulatory proteins including the lactose, galactose, and fructose repressors of E. coli. Cluster 3 proteins are specific for histidine, lysine-arginine-ornithine, glutamine, octopine, nopaline, and basic amino acids. Cluster 4 proteins are specific for leucine and leucine-isoleucine-valine, and they are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. Cluster 5 proteins are specific for dipeptides and oligopeptides as well as nickel. Cluster 6 proteins are specific for sulfate, thiosulfate, and possibly phosphate. Cluster 7 proteins are specific for dicarboxylates and tricarboxylates, but these two proteins exhibit insufficient sequence similarity to establish homology. Finally, cluster 8 proteins are specific for iron complexes and possibly vitamin B12. Members of each cluster of binding proteins exhibit greater sequence conservation in their N-terminal domains than in their C-terminal domains. Signature sequences for these eight protein families are presented. The results reveal that binding proteins specific for the same solute from different bacteria are generally more closely related to each other than are binding proteins specific for different solutes from the same organism, although exceptions exist. They also suggest that a requirement for high-affinity solute binding imposes severe structural constraints on a protein. The occurrence of two distinct classes of bacterial cytoplasmic repressor proteins which are homologous to two different clusters of periplasmic binding proteins suggests that the gene-splicing events which allowed functional conversion of these proteins with retention of domain structure have occurred repeatedly during evolutionary history.(ABSTRACT TRUNCATED AT 400 WORDS)

Full text

PDF
320

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abouhamad W. N., Manson M., Gibson M. M., Higgins C. F. Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein. Mol Microbiol. 1991 May;5(5):1035–1047. doi: 10.1111/j.1365-2958.1991.tb01876.x. [DOI] [PubMed] [Google Scholar]
  2. Actis L. A., Tolmasky M. E., Farrell D. H., Crosa J. H. Genetic and molecular characterization of essential components of the Vibrio anguillarum plasmid-mediated iron-transport system. J Biol Chem. 1988 Feb 25;263(6):2853–2860. [PubMed] [Google Scholar]
  3. Adams M. D., Oxender D. L. Bacterial periplasmic binding protein tertiary structures. J Biol Chem. 1989 Sep 25;264(27):15739–15742. [PubMed] [Google Scholar]
  4. Adams M. D., Wagner L. M., Graddis T. J., Landick R., Antonucci T. K., Gibson A. L., Oxender D. L. Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli. J Biol Chem. 1990 Jul 15;265(20):11436–11443. [PubMed] [Google Scholar]
  5. Ahlem C., Huisman W., Neslund G., Dahms A. S. Purification and properties of a periplasmic D-xylose-binding protein from Escherichia coli K-12. J Biol Chem. 1982 Mar 25;257(6):2926–2931. [PubMed] [Google Scholar]
  6. Akasaka M., Mizoguchi J., Takahashi K. A human cDNA sequence of a novel glutathione peroxidase-related protein. Nucleic Acids Res. 1990 Aug 11;18(15):4619–4619. doi: 10.1093/nar/18.15.4619. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Alloing G., Trombe M. C., Claverys J. P. The ami locus of the gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of gram-negative bacteria. Mol Microbiol. 1990 Apr;4(4):633–644. doi: 10.1111/j.1365-2958.1990.tb00632.x. [DOI] [PubMed] [Google Scholar]
  8. Ames G. F., Joshi A. K. Energy coupling in bacterial periplasmic permeases. J Bacteriol. 1990 Aug;172(8):4133–4137. doi: 10.1128/jb.172.8.4133-4137.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ames G. F., Lecar H. ATP-dependent bacterial transporters and cystic fibrosis: analogy between channels and transporters. FASEB J. 1992 Jun;6(9):2660–2666. doi: 10.1096/fasebj.6.9.1377140. [DOI] [PubMed] [Google Scholar]
  10. Angerer A., Gaisser S., Braun V. Nucleotide sequences of the sfuA, sfuB, and sfuC genes of Serratia marcescens suggest a periplasmic-binding-protein-dependent iron transport mechanism. J Bacteriol. 1990 Feb;172(2):572–578. doi: 10.1128/jb.172.2.572-578.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ankenbauer R. G., Nester E. W. Sugar-mediated induction of Agrobacterium tumefaciens virulence genes: structural specificity and activities of monosaccharides. J Bacteriol. 1990 Nov;172(11):6442–6446. doi: 10.1128/jb.172.11.6442-6446.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Anraku Y. Transport of sugars and amino acids in bacteria. I. Purification and specificity of the galactose- and leucine-binding proteins. J Biol Chem. 1968 Jun 10;243(11):3116–3122. [PubMed] [Google Scholar]
  13. Argast M., Boos W. Purification and properties of the sn-glycerol 3-phosphate-binding protein of Escherichia coli. J Biol Chem. 1979 Nov 10;254(21):10931–10935. [PubMed] [Google Scholar]
  14. Bairoch A. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 1991 Apr 25;19 (Suppl):2241–2245. doi: 10.1093/nar/19.suppl.2241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Bairoch A. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 1992 May 11;20 (Suppl):2013–2018. doi: 10.1093/nar/20.suppl.2013. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Barash H., Halpern Y. S. Purification and properties of glutamate binding protein from the periplasmic space of Escherichia coli K-12. Biochim Biophys Acta. 1975 Mar 28;386(1):168–180. doi: 10.1016/0005-2795(75)90257-3. [DOI] [PubMed] [Google Scholar]
  17. Bell A. W., Buckel S. D., Groarke J. M., Hope J. N., Kingsley D. H., Hermodson M. A. The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12. J Biol Chem. 1986 Jun 15;261(17):7652–7658. [PubMed] [Google Scholar]
  18. Berger E. A., Heppel L. A. A binding protein involved in the transport of cystine and diaminopimelic acid in Escherichia coli. J Biol Chem. 1972 Dec 10;247(23):7684–7694. [PubMed] [Google Scholar]
  19. Berish S. A., Kapczynski D. R., Morse S. A. Nucleotide sequence of the Fbp gene from Neisseria meningitidis. Nucleic Acids Res. 1990 Aug 11;18(15):4596–4596. doi: 10.1093/nar/18.15.4596. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Bourret R. B., Borkovich K. A., Simon M. I. Signal transduction pathways involving protein phosphorylation in prokaryotes. Annu Rev Biochem. 1991;60:401–441. doi: 10.1146/annurev.bi.60.070191.002153. [DOI] [PubMed] [Google Scholar]
  21. Bradbeer C., Kenley J. S., Di Masi D. R., Leighton M. Transport of vitamin B12 in Escherichia coli. Corrinoid specificities of the periplasmic B12-binding protein and of energy-dependent B12 transport. J Biol Chem. 1978 Mar 10;253(5):1347–1352. [PubMed] [Google Scholar]
  22. Buckenmeyer G. K., Hermodson M. A. The amino acid sequence of D-ribose-binding protein from Salmonella typhimurium ST1. J Biol Chem. 1983 Nov 10;258(21):12957–12957. [PubMed] [Google Scholar]
  23. Burnett W. V., Henner J., Eckhardt T. The nucleotide sequence of the gene coding for XP55, a major secreted protein from Streptomyces lividans. Nucleic Acids Res. 1987 May 11;15(9):3926–3926. doi: 10.1093/nar/15.9.3926. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Callahan H. L., Beverley S. M. Heavy metal resistance: a new role for P-glycoproteins in Leishmania. J Biol Chem. 1991 Oct 5;266(28):18427–18430. [PubMed] [Google Scholar]
  25. Cangelosi G. A., Ankenbauer R. G., Nester E. W. Sugars induce the Agrobacterium virulence genes through a periplasmic binding protein and a transmembrane signal protein. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6708–6712. doi: 10.1073/pnas.87.17.6708. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Cangelosi G. A., Martinetti G., Leigh J. A., Lee C. C., Thienes C., Theines C., Nester E. W. Role for [corrected] Agrobacterium tumefaciens ChvA protein in export of beta-1,2-glucan. J Bacteriol. 1989 Mar;171(3):1609–1615. doi: 10.1128/jb.171.3.1609-1615.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Chen C. J., Chin J. E., Ueda K., Clark D. P., Pastan I., Gottesman M. M., Roninson I. B. Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell. 1986 Nov 7;47(3):381–389. doi: 10.1016/0092-8674(86)90595-7. [DOI] [PubMed] [Google Scholar]
  28. Chen C. M., Misra T. K., Silver S., Rosen B. P. Nucleotide sequence of the structural genes for an anion pump. The plasmid-encoded arsenical resistance operon. J Biol Chem. 1986 Nov 15;261(32):15030–15038. [PubMed] [Google Scholar]
  29. Chen C. M., Ye Q. Z., Zhu Z. M., Wanner B. L., Walsh C. T. Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B. J Biol Chem. 1990 Mar 15;265(8):4461–4471. [PubMed] [Google Scholar]
  30. Coulton J. W., Mason P., Allatt D. D. fhuC and fhuD genes for iron (III)-ferrichrome transport into Escherichia coli K-12. J Bacteriol. 1987 Aug;169(8):3844–3849. doi: 10.1128/jb.169.8.3844-3849.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Cox G. B., Webb D., Godovac-Zimmermann J., Rosenberg H. Arg-220 of the PstA protein is required for phosphate transport through the phosphate-specific transport system in Escherichia coli but not for alkaline phosphatase repression. J Bacteriol. 1988 May;170(5):2283–2286. doi: 10.1128/jb.170.5.2283-2286.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Cox G. B., Webb D., Rosenberg H. Specific amino acid residues in both the PstB and PstC proteins are required for phosphate transport by the Escherichia coli Pst system. J Bacteriol. 1989 Mar;171(3):1531–1534. doi: 10.1128/jb.171.3.1531-1534.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. DREYFUSS J. CHARACTERIZATION OF A SULFATE- AND THIOSULFATE-TRANSPORTING SYSTEM IN SALMONELLA TYPHIMURIUM. J Biol Chem. 1964 Jul;239:2292–2297. [PubMed] [Google Scholar]
  34. Dahl M. K., Francoz E., Saurin W., Boos W., Manson M. D., Hofnung M. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region. Mol Gen Genet. 1989 Aug;218(2):199–207. doi: 10.1007/BF00331269. [DOI] [PubMed] [Google Scholar]
  35. Davidson A. L., Nikaido H. Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli. J Biol Chem. 1990 Mar 15;265(8):4254–4260. [PubMed] [Google Scholar]
  36. Dayhoff M. O., Barker W. C., Hunt L. T. Establishing homologies in protein sequences. Methods Enzymol. 1983;91:524–545. doi: 10.1016/s0076-6879(83)91049-2. [DOI] [PubMed] [Google Scholar]
  37. Dean D. A., Davidson A. L., Nikaido H. Maltose transport in membrane vesicles of Escherichia coli is linked to ATP hydrolysis. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9134–9138. doi: 10.1073/pnas.86.23.9134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Dean D. A., Fikes J. D., Gehring K., Bassford P. J., Jr, Nikaido H. Active transport of maltose in membrane vesicles obtained from Escherichia coli cells producing tethered maltose-binding protein. J Bacteriol. 1989 Jan;171(1):503–510. doi: 10.1128/jb.171.1.503-510.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Dean D. A., Reizer J., Nikaido H., Saier M. H., Jr Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system. Characterization of inducer exclusion-resistant mutants and reconstitution of inducer exclusion in proteoliposomes. J Biol Chem. 1990 Dec 5;265(34):21005–21010. [PubMed] [Google Scholar]
  40. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Doolittle R. F., Feng D. F. Nearest neighbor procedure for relating progressively aligned amino acid sequences. Methods Enzymol. 1990;183:659–669. doi: 10.1016/0076-6879(90)83043-9. [DOI] [PubMed] [Google Scholar]
  42. Doolittle R. F. Similar amino acid sequences: chance or common ancestry? Science. 1981 Oct 9;214(4517):149–159. doi: 10.1126/science.7280687. [DOI] [PubMed] [Google Scholar]
  43. Dreesen T. D., Johnson D. H., Henikoff S. The brown protein of Drosophila melanogaster is similar to the white protein and to components of active transport complexes. Mol Cell Biol. 1988 Dec;8(12):5206–5215. doi: 10.1128/mcb.8.12.5206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Dudler R., Schmidhauser C., Parish R. W., Wettenhall R. E., Schmidt T. A mycoplasma high-affinity transport system and the in vitro invasiveness of mouse sarcoma cells. EMBO J. 1988 Dec 1;7(12):3963–3970. doi: 10.1002/j.1460-2075.1988.tb03283.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Duplay P., Bedouelle H., Fowler A., Zabin I., Saurin W., Hofnung M. Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12. J Biol Chem. 1984 Aug 25;259(16):10606–10613. [PubMed] [Google Scholar]
  46. Endicott J. A., Sarangi F., Ling V. Complete cDNA sequences encoding the Chinese hamster P-glycoprotein gene family. DNA Seq. 1991;2(2):89–101. doi: 10.3109/10425179109039677. [DOI] [PubMed] [Google Scholar]
  47. Evans I. J., Downie J. A. The nodI gene product of Rhizobium leguminosarum is closely related to ATP-binding bacterial transport proteins; nucleotide sequence analysis of the nodI and nodJ genes. Gene. 1986;43(1-2):95–101. doi: 10.1016/0378-1119(86)90012-0. [DOI] [PubMed] [Google Scholar]
  48. Felmlee T., Pellett S., Welch R. A. Nucleotide sequence of an Escherichia coli chromosomal hemolysin. J Bacteriol. 1985 Jul;163(1):94–105. doi: 10.1128/jb.163.1.94-105.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Feng D. F., Doolittle R. F. Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol. 1990;183:375–387. doi: 10.1016/0076-6879(90)83025-5. [DOI] [PubMed] [Google Scholar]
  50. Fikes J. D., Bassford P. J., Jr Export of unprocessed precursor maltose-binding protein to the periplasm of Escherichia coli cells. J Bacteriol. 1987 Jun;169(6):2352–2359. doi: 10.1128/jb.169.6.2352-2359.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Friedrich M. J., de Veaux L. C., Kadner R. J. Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems. J Bacteriol. 1986 Sep;167(3):928–934. doi: 10.1128/jb.167.3.928-934.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Frosch M., Edwards U., Bousset K., Krausse B., Weisgerber C. Evidence for a common molecular origin of the capsule gene loci in gram-negative bacteria expressing group II capsular polysaccharides. Mol Microbiol. 1991 May;5(5):1251–1263. doi: 10.1111/j.1365-2958.1991.tb01899.x. [DOI] [PubMed] [Google Scholar]
  53. Furlong C. E., Weiner J. H. Purification of a leucine-specific binding protein from Escherichia coli. Biochem Biophys Res Commun. 1970 Mar 27;38(6):1076–1083. doi: 10.1016/0006-291x(70)90349-9. [DOI] [PubMed] [Google Scholar]
  54. Furuchi T., Kashiwagi K., Kobayashi H., Igarashi K. Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome. J Biol Chem. 1991 Nov 5;266(31):20928–20933. [PubMed] [Google Scholar]
  55. Gardina P., Conway C., Kossman M., Manson M. Aspartate and maltose-binding protein interact with adjacent sites in the Tar chemotactic signal transducer of Escherichia coli. J Bacteriol. 1992 Mar;174(5):1528–1536. doi: 10.1128/jb.174.5.1528-1536.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Geistlich M., Losick R., Turner J. R., Rao R. N. Characterization of a novel regulatory gene governing the expression of a polyketide synthase gene in Streptomyces ambofaciens. Mol Microbiol. 1992 Jul;6(14):2019–2029. doi: 10.1111/j.1365-2958.1992.tb01374.x. [DOI] [PubMed] [Google Scholar]
  57. Gibson M. M., Price M., Higgins C. F. Genetic characterization and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium. J Bacteriol. 1984 Oct;160(1):122–130. doi: 10.1128/jb.160.1.122-130.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Gilson E., Alloing G., Schmidt T., Claverys J. P., Dudler R., Hofnung M. Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma. EMBO J. 1988 Dec 1;7(12):3971–3974. doi: 10.1002/j.1460-2075.1988.tb03284.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Gilson L., Mahanty H. K., Kolter R. Genetic analysis of an MDR-like export system: the secretion of colicin V. EMBO J. 1990 Dec;9(12):3875–3884. doi: 10.1002/j.1460-2075.1990.tb07606.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Glaser P., Sakamoto H., Bellalou J., Ullmann A., Danchin A. Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. EMBO J. 1988 Dec 1;7(12):3997–4004. doi: 10.1002/j.1460-2075.1988.tb03288.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Goodell E. W., Higgins C. F. Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli. J Bacteriol. 1987 Aug;169(8):3861–3865. doi: 10.1128/jb.169.8.3861-3865.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Gowrishankar J. Nucleotide sequence of the osmoregulatory proU operon of Escherichia coli. J Bacteriol. 1989 Apr;171(4):1923–1931. doi: 10.1128/jb.171.4.1923-1931.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Gros P., Croop J., Housman D. Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell. 1986 Nov 7;47(3):371–380. doi: 10.1016/0092-8674(86)90594-5. [DOI] [PubMed] [Google Scholar]
  64. Gros P., Raymond M., Bell J., Housman D. Cloning and characterization of a second member of the mouse mdr gene family. Mol Cell Biol. 1988 Jul;8(7):2770–2778. doi: 10.1128/mcb.8.7.2770. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Grossman A. D., Losick R. Extracellular control of spore formation in Bacillus subtilis. Proc Natl Acad Sci U S A. 1988 Jun;85(12):4369–4373. doi: 10.1073/pnas.85.12.4369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Guilfoile P. G., Hutchinson C. R. A bacterial analog of the mdr gene of mammalian tumor cells is present in Streptomyces peucetius, the producer of daunorubicin and doxorubicin. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8553–8557. doi: 10.1073/pnas.88.19.8553. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Guyer C. A., Morgan D. G., Osheroff N., Staros J. V. Purification and characterization of a periplasmic oligopeptide binding protein from Escherichia coli. J Biol Chem. 1985 Sep 5;260(19):10812–10818. [PubMed] [Google Scholar]
  68. Gärtner J., Moser H., Valle D. Mutations in the 70K peroxisomal membrane protein gene in Zellweger syndrome. Nat Genet. 1992 Apr;1(1):16–23. doi: 10.1038/ng0492-16. [DOI] [PubMed] [Google Scholar]
  69. Hellinga H. W., Evans P. R. Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase. Eur J Biochem. 1985 Jun 3;149(2):363–373. doi: 10.1111/j.1432-1033.1985.tb08934.x. [DOI] [PubMed] [Google Scholar]
  70. Higgins C. F. ABC transporters: from microorganisms to man. Annu Rev Cell Biol. 1992;8:67–113. doi: 10.1146/annurev.cb.08.110192.000435. [DOI] [PubMed] [Google Scholar]
  71. Higgins C. F., Ames G. F. Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: complete nucleotide sequences. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6038–6042. doi: 10.1073/pnas.78.10.6038. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Higgins C. F., Haag P. D., Nikaido K., Ardeshir F., Garcia G., Ames G. F. Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium. Nature. 1982 Aug 19;298(5876):723–727. doi: 10.1038/298723a0. [DOI] [PubMed] [Google Scholar]
  73. Higgins C. F., Hyde S. C., Mimmack M. M., Gileadi U., Gill D. R., Gallagher M. P. Binding protein-dependent transport systems. J Bioenerg Biomembr. 1990 Aug;22(4):571–592. doi: 10.1007/BF00762962. [DOI] [PubMed] [Google Scholar]
  74. Highlander S. K., Chidambaram M., Engler M. J., Weinstock G. M. DNA sequence of the Pasteurella haemolytica leukotoxin gene cluster. DNA. 1989 Jan-Feb;8(1):15–28. doi: 10.1089/dna.1.1989.8.15. [DOI] [PubMed] [Google Scholar]
  75. Hiles I. D., Gallagher M. P., Jamieson D. J., Higgins C. F. Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J Mol Biol. 1987 May 5;195(1):125–142. doi: 10.1016/0022-2836(87)90332-9. [DOI] [PubMed] [Google Scholar]
  76. Hiles I. D., Higgins C. F. Peptide uptake by Salmonella typhimurium. The periplasmic oligopeptide-binding protein. Eur J Biochem. 1986 Aug 1;158(3):561–567. doi: 10.1111/j.1432-1033.1986.tb09791.x. [DOI] [PubMed] [Google Scholar]
  77. Hoch J. A. Genetics of bacterial sporulation. Adv Genet. 1976;18:69–98. doi: 10.1016/s0065-2660(08)60437-x. [DOI] [PubMed] [Google Scholar]
  78. Hoch J. A. The phosphorelay signal transduction pathway in the initiation of Bacillus subtilis sporulation. J Cell Biochem. 1993 Jan;51(1):55–61. doi: 10.1002/jcb.240510111. [DOI] [PubMed] [Google Scholar]
  79. Hogg R. W., Hermodson M. A. Amino acid sequence of the L-arabinose-binding protein from Escherichia coli B/r. J Biol Chem. 1977 Jul 25;252(14):5135–5141. [PubMed] [Google Scholar]
  80. Hoshino T., Kose-Terai K., Sato K. Solubilization and reconstitution of the Pseudomonas aeruginosa high affinity branched-chain amino acid transport system. J Biol Chem. 1992 Oct 25;267(30):21313–21318. [PubMed] [Google Scholar]
  81. Hoshino T., Kose K. Cloning, nucleotide sequences, and identification of products of the Pseudomonas aeruginosa PAO bra genes, which encode the high-affinity branched-chain amino acid transport system. J Bacteriol. 1990 Oct;172(10):5531–5539. doi: 10.1128/jb.172.10.5531-5539.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Hryniewicz M., Sirko A., Pałucha A., Böck A., Hulanicka D. Sulfate and thiosulfate transport in Escherichia coli K-12: identification of a gene encoding a novel protein involved in thiosulfate binding. J Bacteriol. 1990 Jun;172(6):3358–3366. doi: 10.1128/jb.172.6.3358-3366.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Huang M. L., Cangelosi G. A., Halperin W., Nester E. W. A chromosomal Agrobacterium tumefaciens gene required for effective plant signal transduction. J Bacteriol. 1990 Apr;172(4):1814–1822. doi: 10.1128/jb.172.4.1814-1822.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Isihara H., Hogg R. W. Amino acid sequence of the sulfate-binding protein from Salmonella typhimurium LT2. J Biol Chem. 1980 May 25;255(10):4614–4618. [PubMed] [Google Scholar]
  85. Iwashima A., Matsuura A., Nose Y. Thiamine-binding protein of Escherichia coli. J Bacteriol. 1971 Dec;108(3):1419–1421. doi: 10.1128/jb.108.3.1419-1421.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. 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]
  87. Ji G., Silver S. Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9474–9478. doi: 10.1073/pnas.89.20.9474. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Kamijo K., Taketani S., Yokota S., Osumi T., Hashimoto T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily. J Biol Chem. 1990 Mar 15;265(8):4534–4540. [PubMed] [Google Scholar]
  89. Kanehisa M. I. Los Alamos sequence analysis package for nucleic acids and proteins. Nucleic Acids Res. 1982 Jan 11;10(1):183–196. doi: 10.1093/nar/10.1.183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Kashiwagi K., Yamaguchi Y., Sakai Y., Kobayashi H., Igarashi K. Identification of the polyamine-induced protein as a periplasmic oligopeptide binding protein. J Biol Chem. 1990 May 25;265(15):8387–8391. [PubMed] [Google Scholar]
  91. Kellermann O., Szmelcman S. Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein. Eur J Biochem. 1974 Aug 15;47(1):139–149. doi: 10.1111/j.1432-1033.1974.tb03677.x. [DOI] [PubMed] [Google Scholar]
  92. Kerppola R. E., Ames G. F. Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family. J Biol Chem. 1992 Feb 5;267(4):2329–2336. [PubMed] [Google Scholar]
  93. Kossmann M., Wolff C., Manson M. D. Maltose chemoreceptor of Escherichia coli: interaction of maltose-binding protein and the tar signal transducer. J Bacteriol. 1988 Oct;170(10):4516–4521. doi: 10.1128/jb.170.10.4516-4521.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Krishnan M., Burgner J. W., Chilton W. S., Gelvin S. B. Transport of nonmetabolizable opines by Agrobacterium tumefaciens. J Bacteriol. 1991 Jan;173(2):903–905. doi: 10.1128/jb.173.2.903-905.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Kroll J. S., Hopkins I., Moxon E. R. Capsule loss in H. influenzae type b occurs by recombination-mediated disruption of a gene essential for polysaccharide export. Cell. 1988 May 6;53(3):347–356. doi: 10.1016/0092-8674(88)90155-9. [DOI] [PubMed] [Google Scholar]
  96. Kroll J. S., Loynds B., Brophy L. N., Moxon E. R. The bex locus in encapsulated Haemophilus influenzae: a chromosomal region involved in capsule polysaccharide export. Mol Microbiol. 1990 Nov;4(11):1853–1862. doi: 10.1111/j.1365-2958.1990.tb02034.x. [DOI] [PubMed] [Google Scholar]
  97. Kuchler K., Sterne R. E., Thorner J. Saccharomyces cerevisiae STE6 gene product: a novel pathway for protein export in eukaryotic cells. EMBO J. 1989 Dec 20;8(13):3973–3984. doi: 10.1002/j.1460-2075.1989.tb08580.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. 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]
  99. Köster W. L., Actis L. A., Waldbeser L. S., Tolmasky M. E., Crosa J. H. Molecular characterization of the iron transport system mediated by the pJM1 plasmid in Vibrio anguillarum 775. J Biol Chem. 1991 Dec 15;266(35):23829–23833. [PubMed] [Google Scholar]
  100. Köster W., Braun V. Iron hydroxamate transport of Escherichia coli: nucleotide sequence of the fhuB gene and identification of the protein. Mol Gen Genet. 1986 Sep;204(3):435–442. doi: 10.1007/BF00331021. [DOI] [PubMed] [Google Scholar]
  101. Lacks S. A., Dunn J. J., Greenberg B. Identification of base mismatches recognized by the heteroduplex-DNA-repair system of Streptococcus pneumoniae. Cell. 1982 Dec;31(2 Pt 1):327–336. doi: 10.1016/0092-8674(82)90126-x. [DOI] [PubMed] [Google Scholar]
  102. Landick R., Oxender D. L. The complete nucleotide sequences of the Escherichia coli LIV-BP and LS-BP genes. Implications for the mechanism of high-affinity branched-chain amino acid transport. J Biol Chem. 1985 Jul 15;260(14):8257–8261. [PubMed] [Google Scholar]
  103. Laudenbach D. E., Grossman A. R. Characterization and mutagenesis of sulfur-regulated genes in a cyanobacterium: evidence for function in sulfate transport. J Bacteriol. 1991 May;173(9):2739–2750. doi: 10.1128/jb.173.9.2739-2750.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Lavitola A., Vanni M., Martin P. M., Bruni C. B. Cloning and characterization of a Neisseria gene homologous to hisJ and argT of Escherichia coli and Salmonella typhimurium. Res Microbiol. 1992 Mar-Apr;143(3):295–305. doi: 10.1016/0923-2508(92)90021-f. [DOI] [PubMed] [Google Scholar]
  105. Leive L., Davis B. D. The transport of diaminopimelate and cystine in Escherichia coli. J Biol Chem. 1965 Nov;240(11):4362–4369. [PubMed] [Google Scholar]
  106. Lipman D. J., Pearson W. R. Rapid and sensitive protein similarity searches. Science. 1985 Mar 22;227(4693):1435–1441. doi: 10.1126/science.2983426. [DOI] [PubMed] [Google Scholar]
  107. Lukat G. S., Stock J. B. Response regulation in bacterial chemotaxis. J Cell Biochem. 1993 Jan;51(1):41–46. doi: 10.1002/jcb.240510109. [DOI] [PubMed] [Google Scholar]
  108. Luque F., Mitchenall L. A., Chapman M., Christine R., Pau R. N. Characterization of genes involved in molybdenum transport in Azotobacter vinelandii. Mol Microbiol. 1993 Feb;7(3):447–459. doi: 10.1111/j.1365-2958.1993.tb01136.x. [DOI] [PubMed] [Google Scholar]
  109. Létoffé S., Delepelaire P., Wandersman C. Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin. EMBO J. 1990 May;9(5):1375–1382. doi: 10.1002/j.1460-2075.1990.tb08252.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. 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]
  111. Mahoney W. C., Hogg R. W., Hermodson M. A. The amino acid sequence of the D-galactose-binding protein from Escherichia coli B/r. J Biol Chem. 1981 May 10;256(9):4350–4356. [PubMed] [Google Scholar]
  112. Makino K., Kim S. K., Shinagawa H., Amemura M., Nakata A. Molecular analysis of the cryptic and functional phn operons for phosphonate use in Escherichia coli K-12. J Bacteriol. 1991 Apr;173(8):2665–2672. doi: 10.1128/jb.173.8.2665-2672.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  113. Makino K., Shinagawa H., Amemura M., Kawamoto T., Yamada M., Nakata A. Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins. J Mol Biol. 1989 Dec 5;210(3):551–559. doi: 10.1016/0022-2836(89)90131-9. [DOI] [PubMed] [Google Scholar]
  114. 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]
  115. Marger M. D., Saier M. H., Jr A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport. Trends Biochem Sci. 1993 Jan;18(1):13–20. doi: 10.1016/0968-0004(93)90081-w. [DOI] [PubMed] [Google Scholar]
  116. Martineau P., Saurin W., Hofnung M., Spurlino J. C., Quiocho F. A. Progress in the identification of interaction sites on the periplasmic maltose binding protein from E coli. Biochimie. 1990 Jun-Jul;72(6-7):397–402. doi: 10.1016/0300-9084(90)90063-m. [DOI] [PubMed] [Google Scholar]
  117. Mathiopoulos C., Mueller J. P., Slack F. J., Murphy C. G., Patankar S., Bukusoglu G., Sonenshein A. L. A Bacillus subtilis dipeptide transport system expressed early during sporulation. Mol Microbiol. 1991 Aug;5(8):1903–1913. doi: 10.1111/j.1365-2958.1991.tb00814.x. [DOI] [PubMed] [Google Scholar]
  118. Mauzy C. A., Hermodson M. A. Structural and functional analyses of the repressor, RbsR, of the ribose operon of Escherichia coli. Protein Sci. 1992 Jul;1(7):831–842. doi: 10.1002/pro.5560010701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  119. Mauzy C. A., Hermodson M. A. Structural homology between rbs repressor and ribose binding protein implies functional similarity. Protein Sci. 1992 Jul;1(7):843–849. doi: 10.1002/pro.5560010702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. May G., Faatz E., Lucht J. M., Haardt M., Bolliger M., Bremer E. Characterization of the osmoregulated Escherichia coli proU promoter and identification of ProV as a membrane-associated protein. Mol Microbiol. 1989 Nov;3(11):1521–1531. doi: 10.1111/j.1365-2958.1989.tb00138.x. [DOI] [PubMed] [Google Scholar]
  121. McGrath J. P., Varshavsky A. The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein. Nature. 1989 Aug 3;340(6232):400–404. doi: 10.1038/340400a0. [DOI] [PubMed] [Google Scholar]
  122. Metcalf W. W., Wanner B. L. Involvement of the Escherichia coli phn (psiD) gene cluster in assimilation of phosphorus in the form of phosphonates, phosphite, Pi esters, and Pi. J Bacteriol. 1991 Jan;173(2):587–600. doi: 10.1128/jb.173.2.587-600.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Mietzner T. A., Bolan G., Schoolnik G. K., Morse S. A. Purification and characterization of the major iron-regulated protein expressed by pathogenic Neisseriae. J Exp Med. 1987 Apr 1;165(4):1041–1057. doi: 10.1084/jem.165.4.1041. [DOI] [PMC free article] [PubMed] [Google Scholar]
  124. Miller D. M., 3rd, Olson J. S., Pflugrath J. W., Quiocho F. A. Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis. J Biol Chem. 1983 Nov 25;258(22):13665–13672. [PubMed] [Google Scholar]
  125. Mowbray S. L., Smith R. D., Cole L. B. Structure of the periplasmic glucose/galactose receptor of Salmonella typhimurium. 1990-1991 WinterReceptor. 1(1-2):41–53. [PubMed] [Google Scholar]
  126. Müller-Hill B. Sequence homology between Lac and Gal repressors and three sugar-binding periplasmic proteins. Nature. 1983 Mar 10;302(5904):163–164. doi: 10.1038/302163a0. [DOI] [PubMed] [Google Scholar]
  127. Newcomer M. E., Gilliland G. L., Quiocho F. A. L-Arabinose-binding protein-sugar complex at 2.4 A resolution. Stereochemistry and evidence for a structural change. J Biol Chem. 1981 Dec 25;256(24):13213–13217. [PubMed] [Google Scholar]
  128. Newcomer M. E., Lewis B. A., Quiocho F. A. The radius of gyration of L-arabinose-binding protein decreases upon binding of ligand. J Biol Chem. 1981 Dec 25;256(24):13218–13222. [PubMed] [Google Scholar]
  129. Nielsen J. B., Caulfield M. P., Lampen J. O. Lipoprotein nature of Bacillus licheniformis membrane penicillinase. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3511–3515. doi: 10.1073/pnas.78.6.3511. [DOI] [PMC free article] [PubMed] [Google Scholar]
  130. Nielsen J. B., Lampen J. O. Glyceride-cysteine lipoproteins and secretion by Gram-positive bacteria. J Bacteriol. 1982 Oct;152(1):315–322. doi: 10.1128/jb.152.1.315-322.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  131. Nikaido H., Saier M. H., Jr Transport proteins in bacteria: common themes in their design. Science. 1992 Nov 6;258(5084):936–942. doi: 10.1126/science.1279804. [DOI] [PubMed] [Google Scholar]
  132. Nishimune T., Hayashi R. Thiamine-binding protein and thiamine uptake by Escherichia coli. Biochim Biophys Acta. 1971 Sep 21;244(3):573–583. doi: 10.1016/0304-4165(71)90074-2. [DOI] [PubMed] [Google Scholar]
  133. Nohno T., Saito T., Hong J. S. Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ). Mol Gen Genet. 1986 Nov;205(2):260–269. doi: 10.1007/BF00430437. [DOI] [PubMed] [Google Scholar]
  134. Nucifora G., Chu L., Silver S., Misra T. K. Mercury operon regulation by the merR gene of the organomercurial resistance system of plasmid pDU1358. J Bacteriol. 1989 Aug;171(8):4241–4247. doi: 10.1128/jb.171.8.4241-4247.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  135. O'Hare K., Murphy C., Levis R., Rubin G. M. DNA sequence of the white locus of Drosophila melanogaster. J Mol Biol. 1984 Dec 15;180(3):437–455. doi: 10.1016/0022-2836(84)90021-4. [DOI] [PubMed] [Google Scholar]
  136. Olson E. R., Dunyak D. S., Jurss L. M., Poorman R. A. Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein. J Bacteriol. 1991 Jan;173(1):234–244. doi: 10.1128/jb.173.1.234-244.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  137. Oshima R. G., Willis R. C., Furlong C. E., Schneider J. A. Binding assays for amino acids. The utilization of a cystine binding protein from Escherichia coli for the determination of acid-soluble cystine in small physiological samples. J Biol Chem. 1974 Oct 10;249(19):6033–6039. [PubMed] [Google Scholar]
  138. Ouellette M., Fase-Fowler F., Borst P. The amplified H circle of methotrexate-resistant leishmania tarentolae contains a novel P-glycoprotein gene. EMBO J. 1990 Apr;9(4):1027–1033. doi: 10.1002/j.1460-2075.1990.tb08206.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  139. Overdier D. G., Olson E. R., Erickson B. D., Ederer M. M., Csonka L. N. Nucleotide sequence of the transcriptional control region of the osmotically regulated proU operon of Salmonella typhimurium and identification of the 5' endpoint of the proU mRNA. J Bacteriol. 1989 Sep;171(9):4694–4706. doi: 10.1128/jb.171.9.4694-4706.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  140. Overduin P., Boos W., Tommassen J. Nucleotide sequence of the ugp genes of Escherichia coli K-12: homology to the maltose system. Mol Microbiol. 1988 Nov;2(6):767–775. doi: 10.1111/j.1365-2958.1988.tb00088.x. [DOI] [PubMed] [Google Scholar]
  141. Pardee A. B. Purification and properties of a sulfate-binding protein from Salmonella typhimurium. J Biol Chem. 1966 Dec 25;241(24):5886–5892. [PubMed] [Google Scholar]
  142. Pavelka M. S., Jr, Wright L. F., Silver R. P. Identification of two genes, kpsM and kpsT, in region 3 of the polysialic acid gene cluster of Escherichia coli K1. J Bacteriol. 1991 Aug;173(15):4603–4610. doi: 10.1128/jb.173.15.4603-4610.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  143. Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444–2448. doi: 10.1073/pnas.85.8.2444. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Penrose W. R., Nichoalds G. E., Piperno J. R., Oxender D. L. Purification and properties of a leucine-binding protein from Escherichia coli. J Biol Chem. 1968 Nov 25;243(22):5921–5928. [PubMed] [Google Scholar]
  145. Perego M., Higgins C. F., Pearce S. R., Gallagher M. P., Hoch J. A. The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation. Mol Microbiol. 1991 Jan;5(1):173–185. doi: 10.1111/j.1365-2958.1991.tb01838.x. [DOI] [PubMed] [Google Scholar]
  146. Petronilli V., Ames G. F. Binding protein-independent histidine permease mutants. Uncoupling of ATP hydrolysis from transmembrane signaling. J Biol Chem. 1991 Sep 5;266(25):16293–16296. [PubMed] [Google Scholar]
  147. Pistocchi R., Kashiwagi K., Miyamoto S., Nukui E., Sadakata Y., Kobayashi H., Igarashi K. Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome. J Biol Chem. 1993 Jan 5;268(1):146–152. [PubMed] [Google Scholar]
  148. Powis S. H., Mockridge I., Kelly A., Kerr L. A., Glynne R., Gileadi U., Beck S., Trowsdale J. Polymorphism in a second ABC transporter gene located within the class II region of the human major histocompatibility complex. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1463–1467. doi: 10.1073/pnas.89.4.1463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Quiocho F. A. Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria. Philos Trans R Soc Lond B Biol Sci. 1990 Jan 30;326(1236):341–352. doi: 10.1098/rstb.1990.0016. [DOI] [PubMed] [Google Scholar]
  150. ROTMAN B., RADOJKOVIC J. GALACTOSE TRANSPORT IN ESCHERICHIA COLI. THE MECHANISM UNDERLYING THE RETENTION OF INTRACELLULAR GALACTOSE. J Biol Chem. 1964 Oct;239:3153–3156. [PubMed] [Google Scholar]
  151. Randall L. L., Hardy S. J. Unity in function in the absence of consensus in sequence: role of leader peptides in export. Science. 1989 Mar 3;243(4895):1156–1159. doi: 10.1126/science.2646712. [DOI] [PubMed] [Google Scholar]
  152. Reizer A., Pao G. M., Saier M. H., Jr Evolutionary relationships among the permease proteins of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Construction of phylogenetic trees and possible relatedness to proteins of eukaryotic mitochondria. J Mol Evol. 1991 Aug;33(2):179–193. doi: 10.1007/BF02193633. [DOI] [PubMed] [Google Scholar]
  153. Reizer J., Finley K., Kakuda D., MacLeod C. L., Reizer A., Saier M. H., Jr Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria. Protein Sci. 1993 Jan;2(1):20–30. doi: 10.1002/pro.5560020103. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. Reizer J., Reizer A., Saier M. H., Jr A new subfamily of bacterial ABC-type transport systems catalyzing export of drugs and carbohydrates. Protein Sci. 1992 Oct;1(10):1326–1332. doi: 10.1002/pro.5560011012. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. Reizer J., Reizer A., Saier M. H., Jr, Jacobson G. R. A proposed link between nitrogen and carbon metabolism involving protein phosphorylation in bacteria. Protein Sci. 1992 Jun;1(6):722–726. doi: 10.1002/pro.5560010604. [DOI] [PMC free article] [PubMed] [Google Scholar]
  156. Reizer J., Reizer A., Saier M. H., Jr The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus. Res Microbiol. 1990 Nov-Dec;141(9):1061–1067. doi: 10.1016/0923-2508(90)90079-6. [DOI] [PubMed] [Google Scholar]
  157. Riordan J. R., Rommens J. M., Kerem B., Alon N., Rozmahel R., Grzelczak Z., Zielenski J., Lok S., Plavsic N., Chou J. L. Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science. 1989 Sep 8;245(4922):1066–1073. doi: 10.1126/science.2475911. [DOI] [PubMed] [Google Scholar]
  158. Rosen B. P. Basic amino acid transport in Escherichia coli. J Biol Chem. 1971 Jun 10;246(11):3653–3662. [PubMed] [Google Scholar]
  159. 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]
  160. Ross J. I., Eady E. A., Cove J. H., Cunliffe W. J., Baumberg S., Wootton J. C. Inducible erythromycin resistance in staphylococci is encoded by a member of the ATP-binding transport super-gene family. Mol Microbiol. 1990 Jul;4(7):1207–1214. doi: 10.1111/j.1365-2958.1990.tb00696.x. [DOI] [PubMed] [Google Scholar]
  161. Rosteck P. R., Jr, Reynolds P. A., Hershberger C. L. Homology between proteins controlling Streptomyces fradiae tylosin resistance and ATP-binding transport. Gene. 1991 Jun 15;102(1):27–32. doi: 10.1016/0378-1119(91)90533-h. [DOI] [PubMed] [Google Scholar]
  162. Rudner D. Z., LeDeaux J. R., Ireton K., Grossman A. D. The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence. J Bacteriol. 1991 Feb;173(4):1388–1398. doi: 10.1128/jb.173.4.1388-1398.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  163. Russell R. R., Aduse-Opoku J., Sutcliffe I. C., Tao L., Ferretti J. J. A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism. J Biol Chem. 1992 Mar 5;267(7):4631–4637. [PubMed] [Google Scholar]
  164. SICARD A. M. A NEW SYNTHETIC MEDIUM FOR DIPLOCOCCUS PNEUMONIAE, AND ITS USE FOR THE STUDY OF RECIPROCAL TRANSFORMATIONS AT THE AMIA LOCUS. Genetics. 1964 Jul;50:31–44. doi: 10.1093/genetics/50.1.31. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. Saier M. H., Jr, Werner P. K., Müller M. Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process. Microbiol Rev. 1989 Sep;53(3):333–366. doi: 10.1128/mr.53.3.333-366.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  166. Sautereau A. M., Trombe M. C. Electric transmembrane potential mutation and resistance to the cationic and amphiphilic antitumoral drugs derived from pyridocarbazole, 2-N-methylellipticinium and 2-N-methyl-9-hydroxyellipticinium, in Streptococcus pneumoniae. J Gen Microbiol. 1986 Sep;132(9):2637–2641. doi: 10.1099/00221287-132-9-2637. [DOI] [PubMed] [Google Scholar]
  167. Schatz P. J., Beckwith J. Genetic analysis of protein export in Escherichia coli. Annu Rev Genet. 1990;24:215–248. doi: 10.1146/annurev.ge.24.120190.001243. [DOI] [PubMed] [Google Scholar]
  168. Schoner B., Geistlich M., Rosteck P., Jr, Rao R. N., Seno E., Reynolds P., Cox K., Burgett S., Hershberger C. Sequence similarity between macrolide-resistance determinants and ATP-binding transport proteins. Gene. 1992 Jun 15;115(1-2):93–96. doi: 10.1016/0378-1119(92)90545-z. [DOI] [PubMed] [Google Scholar]
  169. Schweizer H., Argast M., Boos W. Characteristics of a binding protein-dependent transport system for sn-glycerol-3-phosphate in Escherichia coli that is part of the pho regulon. J Bacteriol. 1982 Jun;150(3):1154–1163. doi: 10.1128/jb.150.3.1154-1163.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  170. Shamanna D. K., Sanderson K. E. Uptake and catabolism of D-xylose in Salmonella typhimurium LT2. J Bacteriol. 1979 Jul;139(1):64–70. doi: 10.1128/jb.139.1.64-70.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  171. Shaw J. G., Hamblin M. J., Kelly D. J. Purification, characterization and nucleotide sequence of the periplasmic C4-dicarboxylate-binding protein (DctP) from Rhodobacter capsulatus. Mol Microbiol. 1991 Dec;5(12):3055–3062. doi: 10.1111/j.1365-2958.1991.tb01865.x. [DOI] [PubMed] [Google Scholar]
  172. Shea C. M., McIntosh M. A. Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli. Mol Microbiol. 1991 Jun;5(6):1415–1428. doi: 10.1111/j.1365-2958.1991.tb00788.x. [DOI] [PubMed] [Google Scholar]
  173. Shimkets L. J., Kaiser D. Murein components rescue developmental sporulation of Myxococcus xanthus. J Bacteriol. 1982 Oct;152(1):462–470. doi: 10.1128/jb.152.1.462-470.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  174. Shimoda N., Toyoda-Yamamoto A., Nagamine J., Usami S., Katayama M., Sakagami Y., Machida Y. Control of expression of Agrobacterium vir genes by synergistic actions of phenolic signal molecules and monosaccharides. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6684–6688. doi: 10.1073/pnas.87.17.6684. [DOI] [PMC free article] [PubMed] [Google Scholar]
  175. Sicard A. M., Ephrussi-Taylor H. Genetic recombination in DNA-induced transformation of Pneumococcus. II. Mapping the amiA region. Genetics. 1965 Dec;52(6):1207–1227. doi: 10.1093/genetics/52.6.1207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  176. Slack F. J., Mueller J. P., Strauch M. A., Mathiopoulos C., Sonenshein A. L. Transcriptional regulation of a Bacillus subtilis dipeptide transport operon. Mol Microbiol. 1991 Aug;5(8):1915–1925. doi: 10.1111/j.1365-2958.1991.tb00815.x. [DOI] [PubMed] [Google Scholar]
  177. Smith A. N., Boulnois G. J., Roberts I. S. Molecular analysis of the Escherichia coli K5 kps locus: identification and characterization of an inner-membrane capsular polysaccharide transport system. Mol Microbiol. 1990 Nov;4(11):1863–1869. doi: 10.1111/j.1365-2958.1990.tb02035.x. [DOI] [PubMed] [Google Scholar]
  178. Spurlino J. C., Lu G. Y., Quiocho F. A. The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J Biol Chem. 1991 Mar 15;266(8):5202–5219. doi: 10.2210/pdb1mbp/pdb. [DOI] [PubMed] [Google Scholar]
  179. Stanfield S. W., Ielpi L., O'Brochta D., Helinski D. R., Ditta G. S. The ndvA gene product of Rhizobium meliloti is required for beta-(1----2)glucan production and has homology to the ATP-binding export protein HlyB. J Bacteriol. 1988 Aug;170(8):3523–3530. doi: 10.1128/jb.170.8.3523-3530.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  180. Staudenmaier H., Van Hove B., Yaraghi Z., Braun V. Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli. J Bacteriol. 1989 May;171(5):2626–2633. doi: 10.1128/jb.171.5.2626-2633.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  181. Stirling D. A., Hulton C. S., Waddell L., Park S. F., Stewart G. S., Booth I. R., Higgins C. F. Molecular characterization of the proU loci of Salmonella typhimurium and Escherichia coli encoding osmoregulated glycine betaine transport systems. Mol Microbiol. 1989 Aug;3(8):1025–1038. doi: 10.1111/j.1365-2958.1989.tb00253.x. [DOI] [PubMed] [Google Scholar]
  182. Stock J. B., Lukat G. S., Stock A. M. Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks. Annu Rev Biophys Biophys Chem. 1991;20:109–136. doi: 10.1146/annurev.bb.20.060191.000545. [DOI] [PubMed] [Google Scholar]
  183. Stock J. B., Ninfa A. J., Stock A. M. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol Rev. 1989 Dec;53(4):450–490. doi: 10.1128/mr.53.4.450-490.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  184. Strathdee C. A., Lo R. Y. Cloning, nucleotide sequence, and characterization of genes encoding the secretion function of the Pasteurella haemolytica leukotoxin determinant. J Bacteriol. 1989 Feb;171(2):916–928. doi: 10.1128/jb.171.2.916-928.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  185. 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]
  186. 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]
  187. Sweet G. D., Somers J. M., Kay W. W. Purification and properties of a citrate-binding transport component, the C protein of Salmonella typhimurium. Can J Biochem. 1979 Jun;57(6):710–715. doi: 10.1139/o79-089. [DOI] [PubMed] [Google Scholar]
  188. Szmelcman S., Schwartz M., Silhavy T. J., Boos W. Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching. Eur J Biochem. 1976 May 17;65(1):13–19. doi: 10.1111/j.1432-1033.1976.tb10383.x. [DOI] [PubMed] [Google Scholar]
  189. Tata F., Stanier P., Wicking C., Halford S., Kruyer H., Lench N. J., Scambler P. J., Hansen C., Braman J. C., Williamson R. Cloning the mouse homolog of the human cystic fibrosis transmembrane conductance regulator gene. Genomics. 1991 Jun;10(2):301–307. doi: 10.1016/0888-7543(91)90312-3. [DOI] [PubMed] [Google Scholar]
  190. Taylor R. T., Norrell S. A., Hanna M. L. Uptake of cyanocobalamin by Escherichia coli B: some characteristics and evidence for a binding protein. Arch Biochem Biophys. 1972 Feb;148(2):366–381. doi: 10.1016/0003-9861(72)90154-3. [DOI] [PubMed] [Google Scholar]
  191. Thompson J., Donkersloot J. A. Biosynthesis and distribution of N-carboxyalkyl amino acids (opines) in bacteria. Res Microbiol. 1992 Feb;143(2):127–131. doi: 10.1016/0923-2508(92)90001-5. [DOI] [PubMed] [Google Scholar]
  192. Trandinh C. C., Pao G. M., Saier M. H., Jr Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolyl cis-trans isomerases. FASEB J. 1992 Dec;6(15):3410–3420. doi: 10.1096/fasebj.6.15.1464374. [DOI] [PubMed] [Google Scholar]
  193. Treptow N. A., Shuman H. A. Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system. J Mol Biol. 1988 Aug 20;202(4):809–822. doi: 10.1016/0022-2836(88)90560-8. [DOI] [PubMed] [Google Scholar]
  194. Trombe M. C., Lanéelle G., Sicard A. M. Characterization of a Streptococcus pneumoniae mutant with altered electric transmembrane potential. J Bacteriol. 1984 Jun;158(3):1109–1114. doi: 10.1128/jb.158.3.1109-1114.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  195. Trowsdale J., Hanson I., Mockridge I., Beck S., Townsend A., Kelly A. Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters. Nature. 1990 Dec 20;348(6303):741–744. doi: 10.1038/348741a0. [DOI] [PubMed] [Google Scholar]
  196. Valdivia R. H., Wang L., Winans S. C. Characterization of a putative periplasmic transport system for octopine accumulation encoded by Agrobacterium tumefaciens Ti plasmid pTiA6. J Bacteriol. 1991 Oct;173(20):6398–6405. doi: 10.1128/jb.173.20.6398-6405.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  197. Vartak N. B., Reizer J., Reizer A., Gripp J. T., Groisman E. A., Wu L. F., Tomich J. M., Saier M. H., Jr Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res Microbiol. 1991 Nov-Dec;142(9):951–963. doi: 10.1016/0923-2508(91)90005-u. [DOI] [PubMed] [Google Scholar]
  198. Vyas N. K., Vyas M. N., Quiocho F. A. A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis. Nature. 1987 Jun 18;327(6123):635–638. doi: 10.1038/327635a0. [DOI] [PubMed] [Google Scholar]
  199. Vyas N. K., Vyas M. N., Quiocho F. A. Comparison of the periplasmic receptors for L-arabinose, D-glucose/D-galactose, and D-ribose. Structural and Functional Similarity. J Biol Chem. 1991 Mar 15;266(8):5226–5237. [PubMed] [Google Scholar]
  200. Wanner B. L. Gene regulation by phosphate in enteric bacteria. J Cell Biochem. 1993 Jan;51(1):47–54. doi: 10.1002/jcb.240510110. [DOI] [PubMed] [Google Scholar]
  201. Weickert M. J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J Biol Chem. 1992 Aug 5;267(22):15869–15874. [PubMed] [Google Scholar]
  202. Weiner J. H., Furlong C. E., Heppel L. A. A binding protein for L-glutamine and its relation to active transport in E. coli. Arch Biochem Biophys. 1971 Feb;142(2):715–717. doi: 10.1016/0003-9861(71)90538-8. [DOI] [PubMed] [Google Scholar]
  203. Widenhorn K. A., Somers J. M., Kay W. W. Genetic regulation of the tricarboxylate transport operon (tctI) of Salmonella typhimurium. J Bacteriol. 1989 Aug;171(8):4436–4441. doi: 10.1128/jb.171.8.4436-4441.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  204. Wiech H., Klappa P., Zimmerman R. Protein export in prokaryotes and eukaryotes. Theme with variations. FEBS Lett. 1991 Jul 22;285(2):182–188. doi: 10.1016/0014-5793(91)80800-i. [DOI] [PubMed] [Google Scholar]
  205. Willis R. C., Furlong C. E. Purification and properties of a periplasmic glutamate-aspartate binding protein from Escherichia coli K12 strain W3092. J Biol Chem. 1975 Apr 10;250(7):2574–2580. [PubMed] [Google Scholar]
  206. Willis R. C., Furlong C. E. Purification and properties of a ribose-binding protein from Escherichia coli. J Biol Chem. 1974 Nov 10;249(21):6926–6929. [PubMed] [Google Scholar]
  207. Wilson S., Drew R. Cloning and DNA sequence of amiC, a new gene regulating expression of the Pseudomonas aeruginosa aliphatic amidase, and purification of the amiC product. J Bacteriol. 1991 Aug;173(16):4914–4921. doi: 10.1128/jb.173.16.4914-4921.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  208. Winans S. C. Two-way chemical signaling in Agrobacterium-plant interactions. Microbiol Rev. 1992 Mar;56(1):12–31. doi: 10.1128/mr.56.1.12-31.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  209. Wu C. T., Budding M., Griffin M. S., Croop J. M. Isolation and characterization of Drosophila multidrug resistance gene homologs. Mol Cell Biol. 1991 Aug;11(8):3940–3948. doi: 10.1128/mcb.11.8.3940. [DOI] [PMC free article] [PubMed] [Google Scholar]
  210. Wu L., Welker N. E. Cloning and characterization of a glutamine transport operon of Bacillus stearothermophilus NUB36: effect of temperature on regulation of transcription. J Bacteriol. 1991 Aug;173(15):4877–4888. doi: 10.1128/jb.173.15.4877-4888.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  211. Yamaguchi K., Yu F., Inouye M. A single amino acid determinant of the membrane localization of lipoproteins in E. coli. Cell. 1988 May 6;53(3):423–432. doi: 10.1016/0092-8674(88)90162-6. [DOI] [PubMed] [Google Scholar]
  212. Yorifuji T., Lemna W. K., Ballard C. F., Rosenbloom C. L., Rozmahel R., Plavsic N., Tsui L. C., Beaudet A. L. Molecular cloning and sequence analysis of the murine cDNA for the cystic fibrosis transmembrane conductance regulator. Genomics. 1991 Jul;10(3):547–550. doi: 10.1016/0888-7543(91)90434-g. [DOI] [PubMed] [Google Scholar]
  213. Zanker H., von Lintig J., Schröder J. Opine transport genes in the octopine (occ) and nopaline (noc) catabolic regions in Ti plasmids of Agrobacterium tumefaciens. J Bacteriol. 1992 Feb;174(3):841–849. doi: 10.1128/jb.174.3.841-849.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  214. Zhao G. S., Xia T. H., Fischer R. S., Jensen R. A. Cyclohexadienyl dehydratase from Pseudomonas aeruginosa. Molecular cloning of the gene and characterization of the gene product. J Biol Chem. 1992 Feb 5;267(4):2487–2493. [PubMed] [Google Scholar]
  215. Zumft W. G., Viebrock-Sambale A., Braun C. Nitrous oxide reductase from denitrifying Pseudomonas stutzeri. Genes for copper-processing and properties of the deduced products, including a new member of the family of ATP/GTP-binding proteins. Eur J Biochem. 1990 Sep 24;192(3):591–599. doi: 10.1111/j.1432-1033.1990.tb19265.x. [DOI] [PubMed] [Google Scholar]

Articles from Microbiological Reviews are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES