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. 1972 Dec;36(4):558–586. doi: 10.1128/br.36.4.558-586.1972

Linkage map of Salmonella typhimurium, edition IV.

K E Sanderson
PMCID: PMC408332  PMID: 4568764

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Selected References

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

  1. ANAGNOSTOPOULOS C., CRAWFORD I. P. Transformation studies on the linkage of markers in the tryptophan pathway in Bacillus subtilis. Proc Natl Acad Sci U S A. 1961 Mar 15;47:378–390. doi: 10.1073/pnas.47.3.378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ARMSTRONG F. B., WAGNER R. P. ISOLEUCINE-VALINE REQUIRING MUTANTS OF SALMONELLA TYPHIMURIUM. Genetics. 1964 Nov;50:957–965. doi: 10.1093/genetics/50.5.957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Abd-el-Al A., Ingraham J. L. Cold sensitivity and other phenotypes resulting from mutation in pyrA gene. J Biol Chem. 1969 Aug 10;244(15):4039–4045. [PubMed] [Google Scholar]
  4. Adhya S., Cleary P., Campbell A. A deletion analysis of prophage lambda and adjacent genetic regions. Proc Natl Acad Sci U S A. 1968 Nov;61(3):956–962. doi: 10.1073/pnas.61.3.956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Alexander R. R., Calvo J. M. A Salmonella typhimurium locus involved in the regulation of isoleucine, valine and leucine biosynthesis. Genetics. 1969 Mar;61(3):539–556. doi: 10.1093/genetics/61.3.539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Alexander R. R., Calvo J. M., Freundlich M. Mutants of Salmonella typhimurium with an altered leucyl-transfer ribonucleic acid synthetase. J Bacteriol. 1971 Apr;106(1):213–220. doi: 10.1128/jb.106.1.213-220.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ames G. F., Lever J. E. The histidine-binding protein J is a component of histidine transport. Identification of its structural gene, hisJ. J Biol Chem. 1972 Jul 10;247(13):4309–4316. [PubMed] [Google Scholar]
  8. Ames G. F., Lever J. Components of histidine transport: histidine-binding proteins and hisP protein. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1096–1103. doi: 10.1073/pnas.66.4.1096. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ames G. F., Roth J. R. Histidine and aromatic permeases of Salmonella typhimurim. J Bacteriol. 1968 Nov;96(5):1742–1749. doi: 10.1128/jb.96.5.1742-1749.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Anderson E. H. Growth Requirements of Virus-Resistant Mutants of Escherichia Coli Strain "B". Proc Natl Acad Sci U S A. 1946 May;32(5):120–128. doi: 10.1073/pnas.32.5.120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Antón D. N. Histidine regulatory mutants in Salmonella typhimurium. V. Two new classes histidine regulatory mutants. J Mol Biol. 1968 May 14;33(3):533–546. doi: 10.1016/0022-2836(68)90304-5. [DOI] [PubMed] [Google Scholar]
  12. Antón D. N. Osmotic-sensitive mutant of Salmonella typhimurium. J Bacteriol. 1972 Mar;109(3):1273–1283. doi: 10.1128/jb.109.3.1273-1283.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Armstrong F. B., Ishiwa H. Isoleucine-valine requiring mutants of Salmonella typhimurium. 3. Valine-sensitive strains. Genetics. 1971 Feb;67(2):171–182. doi: 10.1093/genetics/67.2.171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Atkins C. G., Armstrong F. B. Electrophoretic study of Salmonella typhimurium-Salmonella montevideo hybrids. Genetics. 1969 Dec;63(4):775–779. doi: 10.1093/genetics/63.4.775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ayling P. D., Chater K. F. The sequence of four structural and two regulatory methionine genes in the Salmonella typhimurium linkage map. Genet Res. 1968 Dec;12(3):341–354. doi: 10.1017/s0016672300011927. [DOI] [PubMed] [Google Scholar]
  16. BECKWITH J. R., PARDEE A. B., AUSTRIAN R., JACOB F. Coordination of the synthesis of the enzymes in the pyrimidine pathway of E. coli. J Mol Biol. 1962 Dec;5:618–634. doi: 10.1016/s0022-2836(62)80090-4. [DOI] [PubMed] [Google Scholar]
  17. BURNS R. O., UMBARGER H. E., GROSS S. R. THE BIOSYNTHESIS OF LEUCINE. III. THE CONVERSION OF ALPHA-HYDROXY-BETA-CARBOXYISOCAPROATE TO ALPHA-KETOISOCAPROATE. Biochemistry. 1963 Sep-Oct;2:1053–1058. doi: 10.1021/bi00905a024. [DOI] [PubMed] [Google Scholar]
  18. Bagdian G., Mäkelä P. H. Antigenic conversion by phage P27. I. Mapping of the prophage attachment site on the Salmonella chromosome. Virology. 1971 Feb;43(2):403–411. doi: 10.1016/0042-6822(71)90312-6. [DOI] [PubMed] [Google Scholar]
  19. Balbinder E., Blume A. J., Weber A., Tamaki H. Polar and antipolar mutants in the tryptophan operon of Salmonella typhimurium. J Bacteriol. 1968 Jun;95(6):2217–2229. doi: 10.1128/jb.95.6.2217-2229.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Balbinder E., Callahan R., 3rd, McCann P. P., Cordaro J. C., Weber A. R., Smith A. M., Angelosanto F. Regulatory mutants of the tryptophan operon of Salmonella typhimurium. Genetics. 1970 Sep;66(1):31–53. doi: 10.1093/genetics/66.1.31. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Baron L. S., Gemski P., Johnson E. M., Wohlhieter J. A. Intergeneric bacterial matings. Bacteriol Rev. 1968 Dec;32(4 Pt 1):362–369. [PMC free article] [PubMed] [Google Scholar]
  22. Bauerle R. H., Margolin P. A multifunctional enzyme complex in the tryptophan pathway of Salmonella typhimurium: comparison of polarity and pseudopolarity mutations. Cold Spring Harb Symp Quant Biol. 1966;31:203–214. doi: 10.1101/sqb.1966.031.01.028. [DOI] [PubMed] [Google Scholar]
  23. Bauerle R. H., Margolin P. Evidence for two sites for initiation of gene expression in the tryptophan operon of Salmonella typhimurium. J Mol Biol. 1967 Jun 28;26(3):423–436. doi: 10.1016/0022-2836(67)90313-0. [DOI] [PubMed] [Google Scholar]
  24. Bauerle R. H., Margolin P. The functional organization of the tryptophan gene cluster in Salmonella typhimurium. Proc Natl Acad Sci U S A. 1966 Jul;56(1):111–118. doi: 10.1073/pnas.56.1.111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Beacham I. R., Eisenstark A., Barth P. T., Pritchard R. H. Deoxynucleoside-sensitive mutants of Salmonella typhimurium. Mol Gen Genet. 1968;102(2):112–127. doi: 10.1007/BF01789138. [DOI] [PubMed] [Google Scholar]
  26. Beck C. F., Ingraham J. L. Location on the chromosome of Salmonella typhimurium of genes governing pyrimidine metabolism. Mol Gen Genet. 1971;111(4):303–316. doi: 10.1007/BF00569782. [DOI] [PubMed] [Google Scholar]
  27. Beck C. F., Ingraham J. L., Neuhard J. Location on the chromosome of Salmonella typhimurium of genes governing pyrimidine metabolism. II. Uridine kinase, cytosine deaminase and thymidine kinase. Mol Gen Genet. 1972;115(3):208–215. doi: 10.1007/BF00268884. [DOI] [PubMed] [Google Scholar]
  28. Beck C. F., Ingraham J. L., Neuhard J., Thomassen E. Metabolism of pyrimidines and pyrimidine nucleosides by Salmonella typhimurium. J Bacteriol. 1972 Apr;110(1):219–228. doi: 10.1128/jb.110.1.219-228.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Becker M. A., Kredich N. M., Tomkins G. M. The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. J Biol Chem. 1969 May 10;244(9):2418–2427. [PubMed] [Google Scholar]
  30. Benzer S. FINE STRUCTURE OF A GENETIC REGION IN BACTERIOPHAGE. Proc Natl Acad Sci U S A. 1955 Jun 15;41(6):344–354. doi: 10.1073/pnas.41.6.344. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Benzinger R., Kleber I. Transfection of Escherichia coli and Salmonella typhimurium spheroplasts: host-controlled restriction of infective bacteriophage P22 deoxyribonucleic acid. J Virol. 1971 Aug;8(2):197–202. doi: 10.1128/jvi.8.2.197-202.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Berkowitz D. D-Mannitol utilization in Salmonella typhimurium. J Bacteriol. 1971 Jan;105(1):232–240. doi: 10.1128/jb.105.1.232-240.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Berst M., Hellerqvist C. G., Lindberg B., Lüderitz O., Svensson S., Westphal O. Structural investigations on T1 lipopolysaccharides. Eur J Biochem. 1969 Dec;11(2):353–359. doi: 10.1111/j.1432-1033.1969.tb00779.x. [DOI] [PubMed] [Google Scholar]
  34. Bezdek M., Amati P. Properties of P22 and A related Salmonella typhimurium phage. I. General features and host specificity. Virology. 1967 Feb;31(2):272–278. doi: 10.1016/0042-6822(67)90171-7. [DOI] [PubMed] [Google Scholar]
  35. Bhattacharya A. K., Chakravorty M. Induction and repression of L-arabinose isomerase in Salmonella typhimurium. J Bacteriol. 1971 Apr;106(1):107–112. doi: 10.1128/jb.106.1.107-112.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Blank J., Hoffee P. Regulatory mutants of the deo regulon in Salmonella typhimurium. Mol Gen Genet. 1972;116(4):291–298. doi: 10.1007/BF00270086. [DOI] [PubMed] [Google Scholar]
  37. Blasi F., Aloj S. M., Goldberger R. F. Effect of histidine on the enzyme which catalyzes the first step of histidine biosynthesis in Salmonella typhimurium. Biochemistry. 1971 Apr 13;10(8):1409–1417. doi: 10.1021/bi00784a021. [DOI] [PubMed] [Google Scholar]
  38. Blasi F., Barton R. W., Kovach J. S., Goldberger R. F. Interaction between the first enzyme for histidine biosynthesis and histidyl transfer ribonucleic acid. J Bacteriol. 1971 May;106(2):508–513. doi: 10.1128/jb.106.2.508-513.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Blatt J. M., Umbarger H. E. On the role of isoleucyl-tRNA synthetase in multivalent repression. Biochem Genet. 1972 Apr;6(2):99–118. doi: 10.1007/BF00486395. [DOI] [PubMed] [Google Scholar]
  40. Blume A. J., Balbinder E. The tryptophan operon of Salmonella typhimurium. Fine structure analysis by deletion mapping and abortive transduction. Genetics. 1966 Mar;53(3):577–592. doi: 10.1093/genetics/53.3.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Blume A. J., Weber A., Balbinder E. Analysis of polar and nonpolar tryptophan mutants by derepression kinetics. J Bacteriol. 1968 Jun;95(6):2230–2241. doi: 10.1128/jb.95.6.2230-2241.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Boro H., Brenchley J. E. A new generalized transducing phage for Salmonella typhimurium LT2. Virology. 1971 Sep;45(3):835–836. doi: 10.1016/0042-6822(71)90208-x. [DOI] [PubMed] [Google Scholar]
  43. Brenner M., De Lorenzo F., Ames B. N. Energy charge and protein synthesis. Control of aminoacyl transfer ribonucleic acid synthetases. J Biol Chem. 1970 Jan 25;245(2):450–452. [PubMed] [Google Scholar]
  44. Brill W. J., Magasanik B. Genetic and metabolic control of histidase and urocanase in Salmonella typhimurium, strain 15-59. J Biol Chem. 1969 Oct 10;244(19):5392–5402. [PubMed] [Google Scholar]
  45. Burns R. O., Calvo J., Margolin P., Umbarger H. E. Expression of the leucine operon. J Bacteriol. 1966 Apr;91(4):1570–1576. doi: 10.1128/jb.91.4.1570-1576.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Burns R. O., Zarlengo M. H. Threonine deaminase from Salmonella typhimurium. I. Purification and properties. J Biol Chem. 1968 Jan 10;243(1):178–185. [PubMed] [Google Scholar]
  47. Calvo J. M., Freundlich M., Umbarger H. E. Regulation of branched-chain amino acid biosynthesis in Salmonella typhimurium: isolation of regulatory mutants. J Bacteriol. 1969 Mar;97(3):1272–1282. doi: 10.1128/jb.97.3.1272-1282.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Calvo J. M., Morgolin P., Umbarger H. E. Operator constitutive mutations in the leucine operon of Salmonella typhimurium. Genetics. 1969 Apr;61(4):777–787. doi: 10.1093/genetics/61.4.777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Calvo J. M., Worden H. E. A multisite-mutation map of the leucine operon of Salmonella typhimurium. Genetics. 1970 Feb;64(2):199–214. doi: 10.1093/genetics/64.2.199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Carrillo-Castañeda G., Ortega M. V. Mutants of Salmonella typhimurium lacking phosphoenolpyruvate carboxykinase and alpha-ketoglutarate dehydrogenase activities. J Bacteriol. 1970 May;102(2):524–530. doi: 10.1128/jb.102.2.524-530.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Casse F., Pascal M. C., Chippaux M. A mutant of Salmonella typhimurium deficient in tetrathionate reductase activity. Mol Gen Genet. 1972;119(1):71–74. doi: 10.1007/BF00270446. [DOI] [PubMed] [Google Scholar]
  52. Casse F., Pascal M. C., Chippaux M., Ratouchniak J. Mapping of the chl-B gene in Salmonella typhimurium LT2. Mol Gen Genet. 1972;119(1):67–70. doi: 10.1007/BF00270445. [DOI] [PubMed] [Google Scholar]
  53. Cauthen S. E., Foster M. A., Woods D. D. Methionine synthesis by extracts of Salmonella typhimurium. Biochem J. 1966 Feb;98(2):630–635. doi: 10.1042/bj0980630. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Chang G. W., Roth J. R., Ames B. N. Histidine regulation in Salmonella typhimurium. 8. Mutations of the hisT gene. J Bacteriol. 1971 Oct;108(1):410–414. doi: 10.1128/jb.108.1.410-414.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Chater K. F. Dominance of the wild-type alleles of methionine regulatory genes in Salmonella typhimurium. J Gen Microbiol. 1970 Sep;63(1):95–109. doi: 10.1099/00221287-63-1-95. [DOI] [PubMed] [Google Scholar]
  56. Chater K. F., Lawrence D. A., Rowbury R. J., Gross T. S. Suppression of methionyl transfer RNA synthetase mutants of Salmonella typhimurium by methionine regulatory mutations. J Gen Microbiol. 1970 Sep;63(1):121–131. doi: 10.1099/00221287-63-1-121. [DOI] [PubMed] [Google Scholar]
  57. Chater K. F., Rowbury R. J. A genetical study of the feedback-sensitive enzyme of methionine synthesis in Salmonella typhimurium. J Gen Microbiol. 1970 Sep;63(1):111–120. doi: 10.1099/00221287-63-1-111. [DOI] [PubMed] [Google Scholar]
  58. Childs J. D., Smith D. A. New methionine structural gene in Salmonella typhimurium. J Bacteriol. 1969 Oct;100(1):377–382. doi: 10.1128/jb.100.1.377-382.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Chippaux M., Casse F., Pascal M. C. Isolation and phenotypes of mutants from Salmonella typhimurium defective in formate hydrogenlyase activity. J Bacteriol. 1972 May;110(2):766–768. doi: 10.1128/jb.110.2.766-768.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Coleman M. S., Soucie W. G., Armstrong F. B. Branched chain amino acid aminotransferase of Salmonella typhimurium. II. Kinetic comparison with the enzyme from Salmonella montevideo. J Biol Chem. 1971 Mar 10;246(5):1310–1312. [PubMed] [Google Scholar]
  61. Colson A. M., Colson C. Expression of the Escherichia coli K, B and phage P1 DNA host specificities in Salmonella typhimurium. J Gen Microbiol. 1972 Apr;70(1):123–128. doi: 10.1099/00221287-70-1-123. [DOI] [PubMed] [Google Scholar]
  62. Colson A. M., Colson C., Van Pel A. Host-controlled restriction mutants of Salmonella typhimurium. J Gen Microbiol. 1969 Sep;58(1):57–64. doi: 10.1099/00221287-58-1-57. [DOI] [PubMed] [Google Scholar]
  63. Colson C., Colson A. M. A new Salmonella typhimurium DNA host specificity. J Gen Microbiol. 1971 Dec;69(3):345–351. doi: 10.1099/00221287-69-3-345. [DOI] [PubMed] [Google Scholar]
  64. Colson C., Colson A. M., Van Pel A. Chromosomal location of host specificity in Salmonella typhimurium. J Gen Microbiol. 1970 Feb;60(2):265–271. doi: 10.1099/00221287-60-2-265. [DOI] [PubMed] [Google Scholar]
  65. Cordaro J. C., Balbinder E. Evidence for the separability of the operator from the first structural gene in the tryptophan operon of Salmonella typhimurium. Genetics. 1971 Feb;67(2):151–169. doi: 10.1093/genetics/67.2.151. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Cordaro J. C., Roseman S. Deletion mapping of the genes coding for HPr and enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system in Salmonella typhimurium. J Bacteriol. 1972 Oct;112(1):17–29. doi: 10.1128/jb.112.1.17-29.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Corwin L. M., Fanning G. R., Feldman F., Margolin P. Mutation leading to increased sensitivity to chromium in Salmonella typhimurium. J Bacteriol. 1966 Apr;91(4):1509–1515. doi: 10.1128/jb.91.4.1509-1515.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. DELAVIER-KLUTCHKO C., FLAVIN M. ROLE OF A BACTERIAL CYSTATHIONINE-BETA-CLEAVAGE ENZYME IN DISULFIDE DECOMPOSITION. Biochim Biophys Acta. 1965 May 18;99:375–377. doi: 10.1016/s0926-6593(65)80137-0. [DOI] [PubMed] [Google Scholar]
  69. DEMEREC M., GILLESPIE D. H., MIZOBUCHI K. GENETIC STRUCTURE OF THE CYST REGION OF THE SALMONELLA GENOME. Genetics. 1963 Aug;48:997–1009. doi: 10.1093/genetics/48.8.997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. DEMEREC M., OHTA N. GENETIC ANALYSES OF SALMONELLA TYPHIMURIUM X ESCHERICHIA COLI HYBRIDS. Proc Natl Acad Sci U S A. 1964 Aug;52:317–323. doi: 10.1073/pnas.52.2.317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. DREYFUSS J. CHARACTERIZATION OF A SULFATE- AND THIOSULFATE-TRANSPORTING SYSTEM IN SALMONELLA TYPHIMURIUM. J Biol Chem. 1964 Jul;239:2292–2297. [PubMed] [Google Scholar]
  72. Dalal F. R., Gots R. E., Gots J. S. Mechanism of adenine inhibition in adenine-sensitive mutants of Salmonella typhimurium. J Bacteriol. 1966 Feb;91(2):507–513. doi: 10.1128/jb.91.2.507-513.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. De Lorenzo F., Ames B. N. Histidine regulation in Salmonella typhimurium. VII. Purification and general properties of the histidyl transfer ribonucleic acid synthetase. J Biol Chem. 1970 Apr 10;245(7):1710–1716. [PubMed] [Google Scholar]
  74. Demerec M., Adelberg E. A., Clark A. J., Hartman P. E. A proposal for a uniform nomenclature in bacterial genetics. Genetics. 1966 Jul;54(1):61–76. doi: 10.1093/genetics/54.1.61. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Demerec M. Induced Mutations and Possible Mechanisms of the Transmission of Heredity in Escherichia Coli. Proc Natl Acad Sci U S A. 1946 Feb;32(2):36–46. doi: 10.1073/pnas.32.2.36. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Demerec M. Studies of the Streptomycin-Resistance System of Mutations in E. Coli. Genetics. 1951 Nov;36(6):585–597. doi: 10.1093/genetics/36.6.585c. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Dendinger S., Brill W. J. Regulation of proline degradation in Salmonella typhimurium. J Bacteriol. 1970 Jul;103(1):144–152. doi: 10.1128/jb.103.1.144-152.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Dreyfuss J., Pardee A. B. Regulation of sulfate transport in Salmonella typhimurium. J Bacteriol. 1966 Jun;91(6):2275–2280. doi: 10.1128/jb.91.6.2275-2280.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Dröge W., Ruschmann E., Lüderitz O., Westphal O. Biochemical studies on lipopolysaccharides of Salmonella R mutants. 4. Phosphate groups linked to heptose units and their absence in some R lipopolysaccharides. Eur J Biochem. 1968 Mar;4(1):134–138. doi: 10.1111/j.1432-1033.1968.tb00183.x. [DOI] [PubMed] [Google Scholar]
  80. Dubnau E., Margolin P. Suppression of promoter mutations by the pleiotropic supx mutations. Mol Gen Genet. 1972;117(2):91–112. doi: 10.1007/BF00267607. [DOI] [PubMed] [Google Scholar]
  81. Ebel-Tsipis J., Botstein D. Superinfection exclusion by P22 prophage in lysogens of Salmonella typhimurium. 1. Exclusion of generalized transducing particles. Virology. 1971 Sep;45(3):629–637. doi: 10.1016/0042-6822(71)90177-2. [DOI] [PubMed] [Google Scholar]
  82. Eisenstark A., Eisenstark R., Cunningham S. Genetic analysis of thymineless(thy) mutants in Salmonella typhimurium. Genetics. 1968 Apr;58(4):493–506. doi: 10.1093/genetics/58.4.493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Eisenstark A., Eisenstark R., van Dillewijn J., Rörsch A. Radiation--sensitive and recombinationless mutants of Salmonella typhimurium. Mutat Res. 1969 Nov-Dec;8(3):497–504. doi: 10.1016/0027-5107(69)90066-9. [DOI] [PubMed] [Google Scholar]
  84. Elliott C. J., Armstrong F. B. Isoleucine-valine requiring mutants of Salmonella typhimurium. II. Strains deficient in dihydroxyacid dehydratase activity. Genetics. 1968 Feb;58(2):171–179. doi: 10.1093/genetics/58.2.171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Enomoto M. Genetic Studies of Paralyzed Mutants in Salmonella. II. Mapping of Three mot Loci by Linkage Analysis. Genetics. 1966 Nov;54(5):1069–1076. doi: 10.1093/genetics/54.5.1069. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. Enomoto M. Genetic analyses of nonmotile double mutants in Salmonella typhimurium: a new mapping method by abortive transduction. Genetics. 1971 Oct;69(2):145–161. doi: 10.1093/genetics/69.2.145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  87. 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]
  88. Enomoto M., Ishiwa H. A new transducing phage related to P22 of Salmonella typhimurium. J Gen Virol. 1972 Feb;14(2):157–164. doi: 10.1099/0022-1317-14-2-157. [DOI] [PubMed] [Google Scholar]
  89. Enomoto M., Yamaguchi S. Different frequencies of cotransduction of motC and H1 in Salmonella. Genet Res. 1969 Aug;14(1):45–52. doi: 10.1017/s001667230000183x. [DOI] [PubMed] [Google Scholar]
  90. FRAENKEL D., OSBORN M. J., HORECKER B. L., SMITH S. M. Metabolism and cell wall structure of a mutant of Salmonella typhimurium deficient in phosphoglucose isomerase. Biochem Biophys Res Commun. 1963 Jun 20;11:423–428. doi: 10.1016/0006-291x(63)90086-x. [DOI] [PubMed] [Google Scholar]
  91. FUKASAWA T., NIKAIDO H. Galactose mutants of Salmonella typhimurium. Genetics. 1961 Oct;46:1295–1303. doi: 10.1093/genetics/46.10.1295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  92. FUKAZAWA Y., HARTMAN P. E. A P22 BACTERIOPHAGE MUTANT DEFECTIVE IN ANTIGEN CONVERSION. Virology. 1964 Jun;23:279–283. doi: 10.1016/0042-6822(64)90296-x. [DOI] [PubMed] [Google Scholar]
  93. Fankhauser D. B., Hartman P. E. Direct selection for transduction of suppressor mutations and linkage of supD to fla genes in Salmonella. J Bacteriol. 1971 Dec;108(3):1427–1430. doi: 10.1128/jb.108.3.1427-1430.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Fink G. R., Roth J. R. Histidine regulatory mutants in Salmonella typhiumium. VI. Dominance studies. J Mol Biol. 1968 May 14;33(3):547–557. doi: 10.1016/0022-2836(68)90305-7. [DOI] [PubMed] [Google Scholar]
  95. Friedman S. B., Margolin P. Evidence for an altered operator specificity: catabolite repression control of the leucine operon in Salmonella typhimurium. J Bacteriol. 1968 Jun;95(6):2263–2269. doi: 10.1128/jb.95.6.2263-2269.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. GROSS S. R., BURNS R. O., UMBARGER H. E. THE BIOSYNTHESIS OF LEUCINE. II. THE ENZYMIC ISOMERIZATION OF BETA-CARBOXY-BETA-HYDROXYISOCAPROATE AND ALPHA-HYDROXY-BETA-CARBOXYISOCAPROATE. Biochemistry. 1963 Sep-Oct;2:1046–1052. doi: 10.1021/bi00905a023. [DOI] [PubMed] [Google Scholar]
  97. Garibaldi J. A. Influence of temperature on the biosynthesis of iron transport compounds by Salmonella typhimurium. J Bacteriol. 1972 Apr;110(1):262–265. doi: 10.1128/jb.110.1.262-265.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. Glanville E V, Demerec M. Threonine, Isoleucine, and Isoleucine-Valine Mutants of Salmonella Typhimurium. Genetics. 1960 Oct;45(10):1359–1374. doi: 10.1093/genetics/45.10.1359. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Gollub E., Sprinson D. B. A regulatory mutation in tyrosine biosynthesis. Biochem Biophys Res Commun. 1969 May 8;35(3):389–395. doi: 10.1016/0006-291x(69)90511-7. [DOI] [PubMed] [Google Scholar]
  100. Gollub E., Zalkin H., Sprinson D. B. Correlation of genes and enzymes, and studies on regulation of the aromatic pathway in Salmonella. J Biol Chem. 1967 Nov 25;242(22):5323–5328. [PubMed] [Google Scholar]
  101. Gots J. S., Benson C. E., Shumas S. R. Genetic separation of hypoxanthine and guanine-xanthine phosphoribosyltransferase activities by deletion mutations in Salmonella typhimurium. J Bacteriol. 1972 Nov;112(2):910–916. doi: 10.1128/jb.112.2.910-916.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Gots J. S., Dalal F. R., Shumas S. R. Genetic eparation of the inosinic acid cyclohydrolase-transformylase complex of Salmonella typhimurium. J Bacteriol. 1969 Aug;99(2):441–449. doi: 10.1128/jb.99.2.441-449.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Gots J. S., Gollub E. G. SEQUENTIAL BLOCKADE IN ADENINE BIOSYNTHESIS BY GENETIC LOSS OF AN APPARENT BIFUNCTIONAL DEACYLASE. Proc Natl Acad Sci U S A. 1957 Sep 15;43(9):826–834. doi: 10.1073/pnas.43.9.826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Grabner M., Hartman P. E. MG40 phage, a transducing phage related to P22. Virology. 1968 Mar;34(3):521–530. doi: 10.1016/0042-6822(68)90071-8. [DOI] [PubMed] [Google Scholar]
  105. Greeb J., Atkins J. F., Loper J. C. Histidinol dehydrogenase (his D) mutants of Salmonella typhimurium. J Bacteriol. 1971 May;106(2):421–431. doi: 10.1128/jb.106.2.421-431.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  106. Gross T. S., Rowbury R. J. Biochemical and physiological properties of methionyl-sRNA synthetase mutants of Salmonella typhimurium. J Gen Microbiol. 1971 Jan;65(1):5–21. doi: 10.1099/00221287-65-1-5. [DOI] [PubMed] [Google Scholar]
  107. Gross T. S., Rowbury R. J. Methionyl transfer RNA synthetase mutants of Salmonella typhimurium which have normal control of the methionine biosynthetic enzymes. Biochim Biophys Acta. 1969 Jun 17;184(1):233–236. doi: 10.1016/0304-4165(69)90126-3. [DOI] [PubMed] [Google Scholar]
  108. Guggenheim S., Flavin M. Cystathionine gamma-synthase from Salmonella. Beta elimination and replacement reactions and inhibition by O-succinylserine. J Biol Chem. 1969 Jul 10;244(13):3722–3727. [PubMed] [Google Scholar]
  109. HARTMAN P. E., LOPER J. C., SERMAN D. Fine structure mapping by complete transduction between histidine-requiring Salmonella mutants. J Gen Microbiol. 1960 Apr;22:323–353. doi: 10.1099/00221287-22-2-323. [DOI] [PubMed] [Google Scholar]
  110. Hartman P. E., Hartman Z., Stahl R. C. Classification and mapping of spontaneous and induced mutations in the histidine operon of Salmonella. Adv Genet. 1971;16:1–34. doi: 10.1016/s0065-2660(08)60352-1. [DOI] [PubMed] [Google Scholar]
  111. Hatfield G. W., Burns R. O. Specific binding of leucyl transfer RNA to an immature form of L-threonine deaminase: its implications in repression. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1027–1035. doi: 10.1073/pnas.66.4.1027. [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. Hoeksema W. D., Schoenhard D. E. Characterization of a thermolabile sulfite reductase from Salmonella pullorum. J Bacteriol. 1971 Oct;108(1):154–158. doi: 10.1128/jb.108.1.154-158.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  113. Hoffee P. A. 2-deoxyribose gene-enzyme complex in Salmonella typhimurium. I. Isolation and enzymatic characterization of 2-deoxyribose-negative mutants. J Bacteriol. 1968 Feb;95(2):449–457. doi: 10.1128/jb.95.2.449-457.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. Hoffee P. A. 2-deoxyribose-5-phosphate aldolase of Salmonella typhimurium: purification and properties. Arch Biochem Biophys. 1968 Sep 10;126(3):795–802. doi: 10.1016/0003-9861(68)90473-6. [DOI] [PubMed] [Google Scholar]
  115. Hoffee P. A., Robertson B. C. 2-Deoxyribose gene-enzyme complex in Salmonella typhimurium: regulation of phosphodeoxyribomutase. J Bacteriol. 1969 Mar;97(3):1386–1396. doi: 10.1128/jb.97.3.1386-1396.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  116. Hong J. S., Ames B. N. Localized mutagenesis of any specific small region of the bacterial chromosome. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3158–3162. doi: 10.1073/pnas.68.12.3158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Hong J. S., Smith G. R., Ames B. N. Adenosine 3':5'-cyclic monophosphate concentration in the bacterial host regulates the viral decision between lysogeny and lysis. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2258–2262. doi: 10.1073/pnas.68.9.2258. [DOI] [PMC free article] [PubMed] [Google Scholar]
  118. Howe T. G., Dawson G. W. Transduction of pro+ to Salmonella typhimurium proAB47 by phage P22. J Gen Microbiol. 1969 Sep;58(1):65–67. doi: 10.1099/00221287-58-1-65. [DOI] [PubMed] [Google Scholar]
  119. Hwang L. H., Zalkin H. Multiple forms of anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase from Salmonella typhimurium. J Biol Chem. 1971 Apr 25;246(8):2338–2345. [PubMed] [Google Scholar]
  120. Iino T., Enomoto M. Genetical studies of non-flagellate mutants of Salmonella. J Gen Microbiol. 1966 Jun;43(3):315–327. doi: 10.1099/00221287-43-3-315. [DOI] [PubMed] [Google Scholar]
  121. Iino T. Genetics and chemistry of bacterial flagella. Bacteriol Rev. 1969 Dec;33(4):454–475. doi: 10.1128/br.33.4.454-475.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  122. Iino T. A Stabilizer of Antigenic Phases in Salmonella Abortus-Equi. Genetics. 1961 Nov;46(11):1465–1469. doi: 10.1093/genetics/46.11.1465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Ingraham J. L., Neuhard J. Cold-sensitive mutants of Salmonella typhimurium defective in uridine monophosphate kinase (pyrH). J Biol Chem. 1972 Oct 10;247(19):6259–6265. [PubMed] [Google Scholar]
  124. Itikawa H., Demerec M. Ditto deletions in the cysC region of the Salmonella chromosome. Genetics. 1967 Jan;55(1):63–68. doi: 10.1093/genetics/55.1.63. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Itikawa H., Demerec M. Salmonella typhimurium proline mutants. J Bacteriol. 1968 Mar;95(3):1189–1190. doi: 10.1128/jb.95.3.1189-1190.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  126. JOHNSON E. M., KRAUSKOPF B., BARON L. S. GENETIC MAPPING OF VI AND SOMATIC ANTIGENIC DETERMINANTS IN SALMONELLA. J Bacteriol. 1965 Aug;90:302–308. doi: 10.1128/jb.90.2.302-308.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Jargiello P., Hoffee P. Orientation of the deo genes and the serB locus in Salmonella typhimurium. J Bacteriol. 1972 Jul;111(1):296–297. doi: 10.1128/jb.111.1.296-297.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  128. Johnson E. M., Baron L. S. Genetic transfer of the Vi antigen from Salmonella typhosa to Escherichia coli. J Bacteriol. 1969 Jul;99(1):358–359. doi: 10.1128/jb.99.1.358-359.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  129. Johnson E. M., Krauskopf B., Baron L. S. Genetic analysis of the ViA-his chromosomal region in Salmonella. J Bacteriol. 1966 Nov;92(5):1457–1463. doi: 10.1128/jb.92.5.1457-1463.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  130. Joys T. M., Stocker B. A. Recombination in H1, the gene determining the flagellar antigen-i of Salmonella typhimurium; mapping of H1 and fla mutations. J Gen Microbiol. 1969 Oct;58(2):267–275. doi: 10.1099/00221287-58-2-267. [DOI] [PubMed] [Google Scholar]
  131. KELLY M. S., PRITCHARD R. H. UNSTABLE LINKAGE BETWEEN GENETIC MARKERS IN TRANSFORMATION. J Bacteriol. 1965 May;89:1314–1321. doi: 10.1128/jb.89.5.1314-1321.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  132. KIRCHNER C. E. The effects of the mutator gene on molecular changes and mutation of Salmonella typhimurium. J Mol Biol. 1960 Dec;2:331–338. doi: 10.1016/s0022-2836(60)80044-7. [DOI] [PubMed] [Google Scholar]
  133. Kaplan M. M., Flavin M. Cystathionine gamma-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis. J Biol Chem. 1966 Oct 10;241(19):4463–4471. [PubMed] [Google Scholar]
  134. Kaplan M. M., Flavin M. Cystathionine gamma-synthetase of Salmonella. Structural properties of a new enzyme in bacterial methionine biosynthesis. J Biol Chem. 1966 Dec 25;241(24):5781–5789. [PubMed] [Google Scholar]
  135. Kemper J., Margolin P. Suppression by gene substitution for the leuD gene of Salmonella typhimurium. Genetics. 1969 Oct;63(2):263–279. doi: 10.1093/genetics/63.2.263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  136. Kerridge D. Flagellar synthesis in Salmonella typhimurium: factors affecting the formation of the flagellar epsilon-N-methyllysine. J Gen Microbiol. 1966 Jan;42(1):71–82. doi: 10.1099/00221287-42-1-71. [DOI] [PubMed] [Google Scholar]
  137. Kirchner C. E., Rudden M. J. Location of a mutator gene in Salmonella typhimurium by cotransduction. J Bacteriol. 1966 Nov;92(5):1453–1456. doi: 10.1128/jb.92.5.1453-1456.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  138. Krajewska-Grynkiewicz K., Walczak W., Klopotowski T. Mutants of Salmonella typhimurium able to utilize D-histidine as a source of L-histidine. J Bacteriol. 1971 Jan;105(1):28–37. doi: 10.1128/jb.105.1.28-37.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  139. Kredich N. M., Becker M. A., Tomkins G. M. Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium. J Biol Chem. 1969 May 10;244(9):2428–2439. [PubMed] [Google Scholar]
  140. Kredich N. M., Tomkins G. M. The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J Biol Chem. 1966 Nov 10;241(21):4955–4965. [PubMed] [Google Scholar]
  141. Kuo T. T., Stocker B. A. ES18, a general transducing phage for smooth and nonsmooth Salmonella typhimurium. Virology. 1970 Nov;42(3):621–632. doi: 10.1016/0042-6822(70)90308-9. [DOI] [PubMed] [Google Scholar]
  142. Kuo T. T., Stocker B. A. Mapping of rfa Genes in Salmonella typhimurium by ES18 and P22 Transduction and by Conjugation. J Bacteriol. 1972 Oct;112(1):48–57. doi: 10.1128/jb.112.1.48-57.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  143. Kuo T. T., Stocker B. A. Suppression of proline requirement of proA and proAB deletion mutants in Salmonella typhimurium by mutation to arginine requirement. J Bacteriol. 1969 May;98(2):593–598. doi: 10.1128/jb.98.2.593-598.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. LOPER J. C., GRABNAR M., STAHL R. C., HARTMAN Z., HARTMAN P. E. GENES AND PROTEINS INVOLVED IN HISTIDINE BIOSYNTHESIS IN SALMONELLA. Brookhaven Symp Biol. 1964 Dec;17:15–52. [PubMed] [Google Scholar]
  145. LaBrie D. A., Armstrong F. B. Transduction using ilv mutants of Salmonella typhimurium-Salmonella montevideo hybrids. J Bacteriol. 1968 Mar;95(3):1193–1194. doi: 10.1128/jb.95.3.1193-1194.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  146. Lawrence D. A. Regulation of the methionine feedback-sensitive enzyme in mutants of Salmonella typhimurium. J Bacteriol. 1972 Jan;109(1):8–11. doi: 10.1128/jb.109.1.8-11.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  147. Lawrence D. A., Smith D. A., Rowbury R. J. Regulation of methionine synthesis in Salmonella typhimurium: mutants resistant to inhibition by analogues of methionine. Genetics. 1968 Apr;58(4):473–492. doi: 10.1093/genetics/58.4.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Lever J. E. Purification and properties of a component of histidine transport in Salmonella typhimurium. The histidine-binding protein J. J Biol Chem. 1972 Jul 10;247(13):4317–4326. [PubMed] [Google Scholar]
  149. Levinthal M., Nikaido H. Consequences of deletion mutations joining two operons of opposite polarity. J Mol Biol. 1969 Jun 28;42(3):511–520. doi: 10.1016/0022-2836(69)90239-3. [DOI] [PubMed] [Google Scholar]
  150. Levinthal M., Simoni R. D. Genetic analysis of carbohydrate transport-deficient mutants of Salmonella typhimurium. J Bacteriol. 1969 Jan;97(1):250–255. doi: 10.1128/jb.97.1.250-255.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Lewis J. A., Ames B. N. Histidine regulation in Salmonella typhimurium. XI. The percentage of transfer RNA His charged in vivo and its relation to the repression of the histidine operon. J Mol Biol. 1972 Apr 28;66(1):131–142. doi: 10.1016/s0022-2836(72)80011-1. [DOI] [PubMed] [Google Scholar]
  152. Lüderitz O., Staub A. M., Westphal O. Immunochemistry of O and R antigens of Salmonella and related Enterobacteriaceae. Bacteriol Rev. 1966 Mar;30(1):192–255. doi: 10.1128/br.30.1.192-255.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  153. MAKELA P. H. HFR males in Salmonella abony. Genetics. 1963 Mar;48:423–429. doi: 10.1093/genetics/48.3.423. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. MARGOLIN P. Genetic fine structure of the leucine operon in Salmonella. Genetics. 1963 Mar;48:441–457. doi: 10.1093/genetics/48.3.441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. MCDONOUGH M. W. AMINO ACID COMPOSITION OF ANTIGENICALLY DISTINCT SALMONELLA FLAGELLAR PROTEINS. J Mol Biol. 1965 Jun;12:342–355. doi: 10.1016/s0022-2836(65)80258-3. [DOI] [PubMed] [Google Scholar]
  156. Maeba P., Sanwal B. D. Phosphoenolpyruvate carboxylase of Salmonella. Some chemical and allosteric properties. J Biol Chem. 1969 May 25;244(10):2549–2557. [PubMed] [Google Scholar]
  157. Marcus S. L., Balbinder E. Purification of anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase from Salmonella typhimurium using affinity chromatography: resolution of monomeric and dimeric forms. Biochem Biophys Res Commun. 1972 Apr 28;47(2):438–444. doi: 10.1016/0006-291x(72)90733-4. [DOI] [PubMed] [Google Scholar]
  158. Margolies M. N., Goldberger R. F. Correlation between mutation type and the production of cross-reacting material in mutants of the A gene of the histidine operon in Salmonella typhimurium. J Bacteriol. 1968 Feb;95(2):507–519. doi: 10.1128/jb.95.2.507-519.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  159. Margolies M. N., Goldberger R. F. Physical and chemical characterization of the isomerase of histidine biosynthesis in Salmonella typhimurium. J Biol Chem. 1967 Jan 25;242(2):256–264. [PubMed] [Google Scholar]
  160. Martin R. G., Goldberger R. F. Imidazolylacetolphosphate:L-glutamate aminotransferase. Purification and physical properties. J Biol Chem. 1967 Mar 25;242(6):1168–1174. [PubMed] [Google Scholar]
  161. Martin R. G. Polarity in relaxed strains of Salmonella typhimurium. J Mol Biol. 1968 Jan 14;31(1):127–134. doi: 10.1016/0022-2836(68)90060-0. [DOI] [PubMed] [Google Scholar]
  162. Martin R. G., Voll M. J., Appella E. Imidazolylacetolphosphate:L-glutamate aminotransferase. Composition and substructure. J Biol Chem. 1967 Mar 25;242(6):1175–1181. [PubMed] [Google Scholar]
  163. McClatchy J. K., Rickenberg H. V. Heterogeneity of the stability of messenger ribonucleic acid in Salmonella typhimurium. J Bacteriol. 1967 Jan;93(1):115–121. doi: 10.1128/jb.93.1.115-121.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. McGinnis E., Williams L. S. Role of histidine transfer ribonucleic acid in regulation of synthesis of histidyl-transfer ribonucleic acid synthetase of Salmonella typhimurium. J Bacteriol. 1972 Feb;109(2):505–511. doi: 10.1128/jb.109.2.505-511.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. Meiss H. K., Brill W. J., Magasanik B. Genetic control of histidine degradation in Salmonella typhimurium, strain LT-2. J Biol Chem. 1969 Oct 10;244(19):5382–5391. [PubMed] [Google Scholar]
  166. Middleton R. B., Mojica-a T. Genetics of the Enterobacteriaceae. B. Homology in the Enterobacteriaceae based on intercrosses between spaces. Adv Genet. 1971;16:53–79. [PubMed] [Google Scholar]
  167. Mikulka T. W., Stieglitz B. I., Calvo J. M. Leucyl-transfer ribonucleic acid synthetase from a wild-type and temperature-sensitive mutant of Salmonella typhimurium. J Bacteriol. 1972 Feb;109(2):584–593. doi: 10.1128/jb.109.2.584-593.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  168. Miller C. G., Roth J. R. Recessive-lethal nonsense suppressors in Salmonella typhimurium. J Mol Biol. 1971 Jul 14;59(1):63–75. doi: 10.1016/0022-2836(71)90413-x. [DOI] [PubMed] [Google Scholar]
  169. Minson A. C., Smith D. A. Methionine regulatory defects in Salmonella typhimurium arising from amber-suppressible mutations. J Gen Microbiol. 1972 May;70(3):471–476. doi: 10.1099/00221287-70-3-471. [DOI] [PubMed] [Google Scholar]
  170. Miyake T, Demerec M. Proline Mutants of Salmonella Typhimurium. Genetics. 1960 Jun;45(6):755–762. doi: 10.1093/genetics/45.6.755. [DOI] [PMC free article] [PubMed] [Google Scholar]
  171. Mizobuchi K, Demerec M, Gillespie D H. Cysteine Mutants of Salmonella Typhimurium. Genetics. 1962 Nov;47(11):1617–1627. doi: 10.1093/genetics/47.11.1617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Mojica-A T., Middleton R. B. Salmonella typhimurium-Escherichia coli hybrids for the tryptophan region. Genetics. 1972 Aug;71(4):491–505. doi: 10.1093/genetics/71.4.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  173. Mukai F. H., Margolin P. ANALYSIS OF UNLINKED SUPPRESSORS OF AN O degrees MUTATION IN SALMONELLA. Proc Natl Acad Sci U S A. 1963 Jul;50(1):140–148. doi: 10.1073/pnas.50.1.140. [DOI] [PMC free article] [PubMed] [Google Scholar]
  174. Murray M. L., Klopotowski T. Genetic map position of the gluconate-6-phosphate dehydrogenase gene in Salmonella typhimurium. J Bacteriol. 1968 Apr;95(4):1279–1282. doi: 10.1128/jb.95.4.1279-1282.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  175. Mäkelä P. H. Genetic determination of the O antigens of Salmonella groups B (4,5,12) and C1(6,7). J Bacteriol. 1966 Mar;91(3):1115–1125. doi: 10.1128/jb.91.3.1115-1125.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  176. Mäkelä P. H., Jahkola M., Lüderitz O. A new gene cluster rfe concerned with the biosynthesis of Salmonella lipopolysaccharide. J Gen Microbiol. 1970 Jan;60(1):91–106. doi: 10.1099/00221287-60-1-91. [DOI] [PubMed] [Google Scholar]
  177. Mäkelä P. H., Mäkelä O. Salmonella antigen 12-2: genetics of form variation. Ann Med Exp Biol Fenn. 1966;44(2):310–317. [PubMed] [Google Scholar]
  178. Mühlradt P. Biosynthesis of Salmonella lipopolysaccharide. The in vitro transfer of phosphate to the heptose moiety of the core. Eur J Biochem. 1969 Dec;11(2):241–248. doi: 10.1111/j.1432-1033.1969.tb00766.x. [DOI] [PubMed] [Google Scholar]
  179. NAIDE Y., NIKAIDO H., MAEKELAE P. H., WILKINSON R. G., STOCKER B. A. SEMIROUGH STRAINS OF SALMONELLA. Proc Natl Acad Sci U S A. 1965 Jan;53:147–153. doi: 10.1073/pnas.53.1.147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  180. NIKAIDO H., FUKASAWA T. The effect of mutation in a structural gene on the inducibility of the enzymes controlled by other genes of the same operon. Biochem Biophys Res Commun. 1961 Apr 7;4:338–342. doi: 10.1016/0006-291x(61)90214-5. [DOI] [PubMed] [Google Scholar]
  181. Nagano H., Zalkin H., Henderson E. J. The anthranilate synthetase-anthranilate-5-phosphorribosylpyrophosphate phosphoribosyltransferase aggregate. On the reaction mechanism of anthranilate synthetase from Salmonella typhimurium. J Biol Chem. 1970 Aug 10;245(15):3810–3820. [PubMed] [Google Scholar]
  182. Nagano H., Zalkin H. Some physicochemical properties of anthranilate synthetase component I from Salmonella typhimurium. J Biol Chem. 1970 Jun;245(12):3097–3103. [PubMed] [Google Scholar]
  183. Nakae T. Multiple molecular forms of uridine diphosphate glucose pyrophosphorylase from Salmonella typhimurium. 3. Interconversion between various forms. J Biol Chem. 1971 Jul 25;246(14):4404–4411. [PubMed] [Google Scholar]
  184. Nakae T., Nikaido H. Multiple molecular forms of uridine diphosphate glucose pyrophosphorylase from Salmonella typhimurium. II. Genetic determination of multiple forms. J Biol Chem. 1971 Jul 25;246(14):4397–4403. [PubMed] [Google Scholar]
  185. Neuhard J., Ingraham J. Mutants of Salmonella typhimurium requiring cytidine for growth. J Bacteriol. 1968 Jun;95(6):2431–2433. doi: 10.1128/jb.95.6.2431-2433.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  186. Newell S. L., Brill W. J. Mutants of Salmonella typhimurium that are insensitive to catabolite repression of proline degradation. J Bacteriol. 1972 Aug;111(2):375–382. doi: 10.1128/jb.111.2.375-382.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  187. Nijkamp H. J., De Haan P. G. Genetic and biochemical studies of the guanosine 5'-monophosphate pathway in Escherichia coli. Biochim Biophys Acta. 1967 Aug 22;145(1):31–40. doi: 10.1016/0005-2787(67)90651-x. [DOI] [PubMed] [Google Scholar]
  188. Nikaido H., Levinthal M., Nikaido K., Nakane K. Extended deletions in the histidine-rough-B region of the Salmonella chromosome. Proc Natl Acad Sci U S A. 1967 Jun;57(6):1825–1832. doi: 10.1073/pnas.57.6.1825. [DOI] [PMC free article] [PubMed] [Google Scholar]
  189. Nishioka Y., Demerec M., Eisenstark A. Genetic analysis of aromatic mutants of Salmonella typhimurium. Genetics. 1967 Jun;56(2):341–351. doi: 10.1093/genetics/56.2.341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  190. Nishioka Y., Eisenstark A. Sequence of genes replicated in Salmonella typhimurium as examined by transduction techniques. J Bacteriol. 1970 May;102(2):320–333. doi: 10.1128/jb.102.2.320-333.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  191. O'Donovan G. A., Gerhart J. C. Isolation and partial characterization of regulatory mutants of the pyrimidine pathway in Salmonella typhimurium. J Bacteriol. 1972 Mar;109(3):1085–1096. doi: 10.1128/jb.109.3.1085-1096.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  192. O'Donovan G. A., Neuhard J. Pyrimidine metabolism in microorganisms. Bacteriol Rev. 1970 Sep;34(3):278–343. doi: 10.1128/br.34.3.278-343.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  193. O'Neil D. M., Baron L. S., Sypherd P. S. Chromosomal location of ribosomal protein cistrons determined by intergeneric bacterial mating. J Bacteriol. 1969 Jul;99(1):242–247. doi: 10.1128/jb.99.1.242-247.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  194. O'Neill J. P., Freundlich M. Two forms of biosynthetic acetohydroxy acid synthetase in Salmonella typhimurium. Biochem Biophys Res Commun. 1972 Jul 25;48(2):437–443. doi: 10.1016/s0006-291x(72)80070-6. [DOI] [PubMed] [Google Scholar]
  195. OSBORN M. J., ROSEN S. M., ROTHFIELD L., ZELEZNICK L. D., HORECKER B. L. LIPOPOLYSACCHARIDE OF THE GRAM-NEGATIVE CELL WALL. Science. 1964 Aug 21;145(3634):783–789. doi: 10.1126/science.145.3634.783. [DOI] [PubMed] [Google Scholar]
  196. Okada M., Watanabe T., Miyake T. On the nature of the recipient ability of Salmonella typhimurium for foreign deoxyribonucleic acids. J Gen Microbiol. 1968 Feb;50(2):241–252. doi: 10.1099/00221287-50-2-241. [DOI] [PubMed] [Google Scholar]
  197. Okada M., Watanabe T. Transduction with phage PI in Salmonella typhimurium. Nature. 1968 Apr 13;218(5137):185–187. doi: 10.1038/218185a0. [DOI] [PubMed] [Google Scholar]
  198. Osborn M. J. Biochemical characterization of mutants of Salmonella typhimurium lacking glucosyl or galactosyl lipopolysaccharide transferases. Nature. 1968 Mar 9;217(5132):957–960. doi: 10.1038/217957a0. [DOI] [PubMed] [Google Scholar]
  199. Osborn M. J. Structure and biosynthesis of the bacterial cell wall. Annu Rev Biochem. 1969;38:501–538. doi: 10.1146/annurev.bi.38.070169.002441. [DOI] [PubMed] [Google Scholar]
  200. Ota N., Galsworthy P. R., Pardee A. B. Genetics of sulfate transport by Salmonella typhimurium. J Bacteriol. 1971 Mar;105(3):1053–1062. doi: 10.1128/jb.105.3.1053-1062.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  201. PASTERNAK C. A., ELLIS R. J., JONES-MORTIMER M. C., CRICHTON C. E. THE CONTROL OF SULPHATE REDUCTION IN BACTERIA. Biochem J. 1965 Jul;96:270–275. doi: 10.1042/bj0960270. [DOI] [PMC free article] [PubMed] [Google Scholar]
  202. Pardee A. B., Prestidge L. S., Whipple M. B., Dreyfuss J. A binding site for sulfate and its relation to sulfate transport into Salmonella typhimurium. J Biol Chem. 1966 Sep 10;241(17):3962–3969. [PubMed] [Google Scholar]
  203. 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]
  204. Pardee A. B., Watanabe K. Location of sulfate-binding protein in Salmonella typhimurium. J Bacteriol. 1968 Oct;96(4):1049–1054. doi: 10.1128/jb.96.4.1049-1054.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  205. Pearce U. B., Stocker B. A. Phase variation of flagellar antigens in Salmonella: abortive transduction studies. J Gen Microbiol. 1967 Nov;49(2):335–349. doi: 10.1099/00221287-49-2-335. [DOI] [PubMed] [Google Scholar]
  206. Pollack J. R., Ames B. N., Neilands J. B. Iron transport in Salmonella typhimurium: mutants blocked in the biosynthesis of enterobactin. J Bacteriol. 1970 Nov;104(2):635–639. doi: 10.1128/jb.104.2.635-639.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  207. Prell H. H., Bode W. Relation between Px phages and generalised transducing particles of phage P22. Mol Gen Genet. 1971;113(3):214–216. doi: 10.1007/BF00339540. [DOI] [PubMed] [Google Scholar]
  208. Press R., Glansdorff N., Miner P., De Vries J., Kadner R., Maas W. K. Isolation of transducing particles of phi-80 bacteriophage that carry different regions of the Escherichia coli genome. Proc Natl Acad Sci U S A. 1971 Apr;68(4):795–798. doi: 10.1073/pnas.68.4.795. [DOI] [PMC free article] [PubMed] [Google Scholar]
  209. Rao R. N., Smith H. O. Phage P22 lysogens of a Salmonella typhimurium mutant deleted at the normal prophage attachment site. Virology. 1968 Oct;36(2):328–330. doi: 10.1016/0042-6822(68)90157-8. [DOI] [PubMed] [Google Scholar]
  210. Rechler M. M., Bruni C. B. Properties of a fused protein formed by genetic manipulation. Histidinol dehydrogenase-imidazolylacetol phosphate: L-glutamate aminotransferase. J Biol Chem. 1971 Mar 25;246(6):1806–1813. [PubMed] [Google Scholar]
  211. Reeves R. H., Roth J. R. A recessive UGA suppressor. J Mol Biol. 1971 Mar 28;56(3):523–533. doi: 10.1016/0022-2836(71)90399-8. [DOI] [PubMed] [Google Scholar]
  212. Rhoades M., MacHattie L. A., Thomas C. A., Jr The P22 bacteriophage DNA molecule. I. The mature form. J Mol Biol. 1968 Oct 14;37(1):21–40. doi: 10.1016/0022-2836(68)90071-5. [DOI] [PubMed] [Google Scholar]
  213. Riddle D. L., Roth J. R. Frameshift suppressors. 3. Effects of suppressor mutations on transfer RNA. J Mol Biol. 1972 May 28;66(3):495–506. doi: 10.1016/0022-2836(72)90429-9. [DOI] [PubMed] [Google Scholar]
  214. Riddle D. L., Roth J. R. Frameshift suppressors. II. Genetic mapping and dominance studies. J Mol Biol. 1972 May 28;66(3):483–493. doi: 10.1016/0022-2836(72)90428-7. [DOI] [PubMed] [Google Scholar]
  215. Robertson B. C., Jargiello P., Blank J., Hoffee P. A. Genetic regulation of ribonucleoside and deoxyribonucleoside catabolism in Salmonella typhimurium. J Bacteriol. 1970 Jun;102(3):628–635. doi: 10.1128/jb.102.3.628-635.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  216. Roth J. R., Antón D. N., Hartman P. E. Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties. J Mol Biol. 1966 Dec 28;22(2):305–323. doi: 10.1016/0022-2836(66)90134-3. [DOI] [PubMed] [Google Scholar]
  217. Roth J. R., Hartman P. E. Heterogeneity in P22 transducing particles. Virology. 1965 Nov;27(3):297–307. doi: 10.1016/0042-6822(65)90109-1. [DOI] [PubMed] [Google Scholar]
  218. Rothman-Denes L., Martin R. G. Two mutations in the first gene of the histidine operon of Salmonella typhimurium affecting control. J Bacteriol. 1971 Apr;106(1):227–237. doi: 10.1128/jb.106.1.227-237.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  219. Rowbury R. J., Lawrence D. A., Smith D. A. Regulation of the methionine-specific aspartokinase and homoserine dehydrogenase of Salmonella typhimurium. J Gen Microbiol. 1968 Dec;54(3):337–342. doi: 10.1099/00221287-54-3-337. [DOI] [PubMed] [Google Scholar]
  220. SANDERSON K. E., DEMEREC M. THE LINKAGE MAP OF SALMONELLA TYPHIMURIUM. Genetics. 1965 Jun;51:897–913. doi: 10.1093/genetics/51.6.897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  221. Saier M. H., Roseman S. Inducer exclusion and repression of enzyme synthesis in mutants of Salmonella typhimurium defective in enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system. J Biol Chem. 1972 Feb 10;247(3):972–975. [PubMed] [Google Scholar]
  222. Sanderson K. E. Current linkage map of Salmonella typhimurium. Bacteriol Rev. 1970 Jun;34(2):176–193. doi: 10.1128/br.34.2.176-193.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  223. Sanderson K. E., Hall C. A. F-prime factors of Salmonella typhimurium and an inversion between S. typhimurium and Escherichia coli. Genetics. 1970 Feb;64(2):215–228. doi: 10.1093/genetics/64.2.215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  224. Sanderson K. E. Revised linkage map of Salmonella typhimurium. Bacteriol Rev. 1967 Dec;31(4):354–372. doi: 10.1128/br.31.4.354-372.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  225. Sanderson K. E., Ross H., Ziegler L., Mäkelä P. H. F + , Hfr, and F' strains of Salmonella typhimurium and Salmonella abony. Bacteriol Rev. 1972 Dec;36(4):608–637. doi: 10.1128/br.36.4.608-637.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  226. Sanderson K. E., Saeed H. Insertion of the F factor into the cluster of rfa (rough A) genes of Salmonella typhimurium. J Bacteriol. 1972 Oct;112(1):64–73. doi: 10.1128/jb.112.1.64-73.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  227. Sanderson K. E., Saeed Y. A. P22-mediated transduction analysis of the rough A (rfa) region of the chromosome of Salmonella typhimurium. J Bacteriol. 1972 Oct;112(1):58–63. doi: 10.1128/jb.112.1.58-63.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  228. Sarvas M. Inheritance of Salmonella T1 antigen. Ann Med Exp Biol Fenn. 1967;45(4):447–471. [PubMed] [Google Scholar]
  229. Savin M. A., Flavin M., Slaughter C. Regulation of homocysteine biosynthesis in Salmonella typhimurium. J Bacteriol. 1972 Aug;111(2):547–556. doi: 10.1128/jb.111.2.547-556.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  230. Sawyer M. E., Armstrong F. B. Order of the ilv genes of Salmonella montevideo. Mol Gen Genet. 1970;109(4):370–372. doi: 10.1007/BF00267705. [DOI] [PubMed] [Google Scholar]
  231. Schmieger H. A method for detection of phage mutants with altered transducing ability. Mol Gen Genet. 1971;110(4):378–381. doi: 10.1007/BF00438281. [DOI] [PubMed] [Google Scholar]
  232. Schmieger H. The molecular structure of the transducing particles of Salmonella phage P22. II. Density gradient analysis of DNA. Mol Gen Genet. 1970;109(4):323–337. doi: 10.1007/BF00267702. [DOI] [PubMed] [Google Scholar]
  233. Shannon K. P., Rowbury R. J. Alteration of the rate of cell division independent of the rate of DNA synthesis in a mutant of Salmonella typhimurium. Mol Gen Genet. 1972;115(2):122–125. doi: 10.1007/BF00277291. [DOI] [PubMed] [Google Scholar]
  234. Shuster C. W., Rundell K. Resistance of Salmonella typhimurium mutants to galactose death. J Bacteriol. 1969 Oct;100(1):103–109. doi: 10.1128/jb.100.1.103-109.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  235. Silbert D. F., Fink G. R., Ames B. N. Histidine regulatory mutants in Salmonella typhimurium 3. A class of regulatory mutants deficient in tRNA for histidine. J Mol Biol. 1966 Dec 28;22(2):335–347. doi: 10.1016/0022-2836(66)90136-7. [DOI] [PubMed] [Google Scholar]
  236. Simoni R. D., Levinthal M., Kundig F. D., Kundig W., Anderson B., Hartman P. E., Roseman S. Genetic evidence for the role of a bacterial phosphotransferase system in sugar transport. Proc Natl Acad Sci U S A. 1967 Nov;58(5):1963–1970. doi: 10.1073/pnas.58.5.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  237. Singer C. E., Smith G. R., Cortese R., Ames B. N. [Mutant tRNA His ineffective in repression and lacking two pseudouridine modifications]. Nat New Biol. 1972 Jul 19;238(81):72–74. doi: 10.1038/newbio238072a0. [DOI] [PubMed] [Google Scholar]
  238. Smith-Keary P. F. Restricted trandsuction by bacteriophage P22 in Salmonella typhimurium. Genet Res. 1966 Aug;8(1):73–82. doi: 10.1017/s0016672300009927. [DOI] [PubMed] [Google Scholar]
  239. Smith D. A., Childs J. D. Methionine genes and enzymes of Salmonella typhimurium. Heredity (Edinb) 1966 May;21(2):265–286. doi: 10.1038/hdy.1966.22. [DOI] [PubMed] [Google Scholar]
  240. Smith D. A. S-amino acid metabolism and its regulation in Escherichia coli and Salmonella typhimurium. Adv Genet. 1971;16:141–165. doi: 10.1016/s0065-2660(08)60357-0. [DOI] [PubMed] [Google Scholar]
  241. Smith D., Bauerle R. H. The anthranilate synthetase-5-phosphorylribose 1-pyrophosphate phosphoribosyl transferase complex of the tryptophan pathway in Salmonella typhimurium. Purification by the in vitro assembly of its subunits. Biochemistry. 1969 Apr;8(4):1451–1459. doi: 10.1021/bi00832a021. [DOI] [PubMed] [Google Scholar]
  242. Smith G. R., Halpern Y. S., Magasanik B. Genetic and metabolic control of enzymes responsible for histidine degradation in Salmonella typhimurium. 4-imidazolone-5-propionate amidohydrolase and N-formimino-L-glutamate formiminohydrolase. J Biol Chem. 1971 May 25;246(10):3320–3329. [PubMed] [Google Scholar]
  243. Smith G. R., Magasanik B. Nature and self-regulated synthesis of the repressor of the hut operons in Salmonella typhimurium. Proc Natl Acad Sci U S A. 1971 Jul;68(7):1493–1497. doi: 10.1073/pnas.68.7.1493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  244. Smith G. R., Magasanik B. The two operons of the histidine utilization system in Salmonella typhimurium. J Biol Chem. 1971 May 25;246(10):3330–3341. [PubMed] [Google Scholar]
  245. Smith G. R. Specialized transduction of the Salmonella hut operons by coliphage lambda: deletion analysis of the hut operons employing lambda-phut. Virology. 1971 Jul;45(1):208–223. doi: 10.1016/0042-6822(71)90128-0. [DOI] [PubMed] [Google Scholar]
  246. Smith H. O., Levine M. Gene order in prophage P22. Virology. 1965 Oct;27(2):229–231. doi: 10.1016/0042-6822(65)90166-2. [DOI] [PubMed] [Google Scholar]
  247. Spratt B. G., Rowbury R. J. Physiological and genetical studies on a mutant of Salmonella typhimurium which is temperature-sensitive for DNA synthesis. Mol Gen Genet. 1972;114(1):35–49. doi: 10.1007/BF00268745. [DOI] [PubMed] [Google Scholar]
  248. St Pierre M. L. Isolation and mapping of Salmonella typhimurium mutants defective in the utilization of trehalose. J Bacteriol. 1968 Mar;95(3):1185–1186. doi: 10.1128/jb.95.3.1185-1186.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  249. Stern J. R., O'Brien R. W. Oxidation D-malic and beta-alkylmalic acids wild-type and mutant strains of Salmonella typhimurium and by Aerobacter aerogenes. J Bacteriol. 1969 Apr;98(1):147–151. doi: 10.1128/jb.98.1.147-151.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  250. Stieglitz B., Calvo J. M. Effect of 4-azaleucine upon leucine metabolism in Salmonella typhimurium. J Bacteriol. 1971 Oct;108(1):95–104. doi: 10.1128/jb.108.1.95-104.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  251. Stocker B. A., Wilkinson R. G., Mäkelä P. H. Genetic aspects of biosynthesis and structure of Salmonella somatic polysaccharide. Ann N Y Acad Sci. 1966 Jun 30;133(2):334–348. doi: 10.1111/j.1749-6632.1966.tb52375.x. [DOI] [PubMed] [Google Scholar]
  252. Stouthamer A. H. A genetical and biochemical study of chlorate-resistant mutants of Salmonella typhimurium. Antonie Van Leeuwenhoek. 1969;35(4):505–521. doi: 10.1007/BF02219168. [DOI] [PubMed] [Google Scholar]
  253. Stouthamer A. H., Bettenhaussen C. W. Mapping of a gene causing resistance to chlorate in Salmonella typhimurium. Antonie Van Leeuwenhoek. 1970;36(4):555–565. doi: 10.1007/BF02069058. [DOI] [PubMed] [Google Scholar]
  254. Stuttard C. Location of trpR mutations in the serB-thr region of Salmonella typhimurium. J Bacteriol. 1972 Aug;111(2):368–374. doi: 10.1128/jb.111.2.368-374.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  255. Susskind M. M., Wright A., Botstein D. Superinfection exclusion by P22 prophage in lysogens of Salmonella typhimurium. II. Genetic evidence for two exclusion systems. Virology. 1971 Sep;45(3):638–652. doi: 10.1016/0042-6822(71)90178-4. [DOI] [PubMed] [Google Scholar]
  256. Suzuki H., Iino T. An assay for newly synthesized intracellular flagellin. Biochim Biophys Acta. 1966 Jul 27;124(1):212–215. doi: 10.1016/0304-4165(66)90337-0. [DOI] [PubMed] [Google Scholar]
  257. Syvanen J. M., Roth J. R. Structural genes for ornithine transcarbamylase in Salmonella typhimurium and Escherichia coli K-12. J Bacteriol. 1972 Apr;110(1):66–70. doi: 10.1128/jb.110.1.66-70.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  258. Săsărman A., Sanderson K. E., Surdeanu M., Sonea S. Hemin-deficient mutants of Salmonella typhimurium. J Bacteriol. 1970 May;102(2):531–536. doi: 10.1128/jb.102.2.531-536.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  259. TAYLOR A. L., THOMAN M. S. THE GENETIC MAP OF ESCHERICHIA COLI K-12. Genetics. 1964 Oct;50:659–677. doi: 10.1093/genetics/50.4.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  260. THEODORE T. S., ENGLESBERG E. MUTANT OF SALMONELLA TYPHIMURIUM DEFICIENT IN THE CARBON DIOXIDE-FIXING ENZYME PHOSPHOENOLPYRUVIC CARBOXYLASE. J Bacteriol. 1964 Oct;88:946–955. doi: 10.1128/jb.88.4.946-955.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  261. Tai P. C., Kessler D. P., Ingraham J. Cold-sensitive mutations in Salmonella typhimurium which affect ribosome synthesis. J Bacteriol. 1969 Mar;97(3):1298–1304. doi: 10.1128/jb.97.3.1298-1304.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  262. Taylor A. L. Current linkage map of Escherichia coli. Bacteriol Rev. 1970 Jun;34(2):155–175. doi: 10.1128/br.34.2.155-175.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  263. Taylor A. L., Trotter C. D. Revised linkage map of Escherichia coli. Bacteriol Rev. 1967 Dec;31(4):332–353. doi: 10.1128/br.31.4.332-353.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  264. Taylor R. T., Weissbach H. N5-methyltetrahydrofolate-homocysteine transmethylase. Partial purification and properties. J Biol Chem. 1967 Apr 10;242(7):1502–1508. [PubMed] [Google Scholar]
  265. Thorne G. M., Corwin L. M. Genetic locus of a gene affecting leucine transport in Salmonella typhimurium. J Bacteriol. 1972 May;110(2):784–785. doi: 10.1128/jb.110.2.784-785.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  266. UMBARGER H. E., UMBARGER M. A., SIU P. M. BIOSYNTHESIS OF SERINE IN ESCHERICHIA COLI AND SALMONELLA TYPHIMURIUM. J Bacteriol. 1963 Jun;85:1431–1439. doi: 10.1128/jb.85.6.1431-1439.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  267. Voll M. J. Translation and polarity in the histidine operon. 3. The isolation of prototrophic polar mutations. J Mol Biol. 1967 Nov 28;30(1):109–124. doi: 10.1016/0022-2836(67)90247-1. [DOI] [PubMed] [Google Scholar]
  268. Westby C. A., Gots J. S. Genetic blocks and unique features in the biosynthesis of 5'-phosphoribosyl-N-formylglycinamide in Salmonella typhimurium. J Biol Chem. 1969 Apr 25;244(8):2095–2102. [PubMed] [Google Scholar]
  269. Wilkinson R. G., Gemski P., Jr, Stocker B. A. Non-smooth mutants of Salmonella typhimurium: differentiation by phage sensitivity and genetic mapping. J Gen Microbiol. 1972 May;70(3):527–554. doi: 10.1099/00221287-70-3-527. [DOI] [PubMed] [Google Scholar]
  270. Wilkinson R. G., Stocker B. A. Genetics and cultural properties of mutants of Salmonella typhimurium lacking glucosyl or galactosyl lipopolysaccharide transferases. Nature. 1968 Mar 9;217(5132):955–957. doi: 10.1038/217955a0. [DOI] [PubMed] [Google Scholar]
  271. Wing J. P., Levine M., Smith H. O. Recombination-deficient mutant of Salmonella typhimurium. J Bacteriol. 1968 May;95(5):1828–1834. doi: 10.1128/jb.95.5.1828-1834.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  272. Wolf R. E., Jr, Loper J. C. The differential inactivation of histidinol dehydrogenase from Salmonella typhimurium by sulfhydryl reagents. J Biol Chem. 1969 Nov 25;244(22):6297–6303. [PubMed] [Google Scholar]
  273. YANOFSKY C., LENNOX E. S. Transduction and recombination study of linkage relationships among the genes controlling tryptophan synthesis in Escherichia coli. Virology. 1959 Aug;8:425–447. doi: 10.1016/0042-6822(59)90046-7. [DOI] [PubMed] [Google Scholar]
  274. YOSHIKAWA H., SUEOKA N. Sequential replication of Bacillus subtilis chromosome. I. Comparison of marker frequencies in exponential and stationary growth phases. Proc Natl Acad Sci U S A. 1963 Apr;49:559–566. doi: 10.1073/pnas.49.4.559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  275. Yamada T., Davies J. A genetic and biochemical study of streptomycin- and spectinomycin-resistance in Salmonella typhimurium. Mol Gen Genet. 1971;110(3):197–210. doi: 10.1007/BF00337833. [DOI] [PubMed] [Google Scholar]
  276. Yamaguchi S., Iino T. Genetic determination of the antigenic specificity of flagellar protein in salmonella. J Gen Microbiol. 1969 Jan;55(1):59–74. doi: 10.1099/00221287-55-1-59. [DOI] [PubMed] [Google Scholar]
  277. Yamaguchi S., Iino T., Horiguchi T., Ota K. Genetic analysis of fla and mot cistrons closely linked to H1 in Salmonella abortusequi and its derivatives. J Gen Microbiol. 1972 Apr;70(1):59–75. doi: 10.1099/00221287-70-1-59. [DOI] [PubMed] [Google Scholar]
  278. Yamaguchi S., Iino T. Serological and finger-printing analyses of mutant flagellar antigens of Salmonella. J Gen Microbiol. 1970 Dec;64(3):311–318. doi: 10.1099/00221287-64-3-311. [DOI] [PubMed] [Google Scholar]
  279. Yan Y., Demerec M. Genetic analysis of pyrimidine mutants of Salmonella typhimurium. Genetics. 1965 Sep;52(3):643–651. doi: 10.1093/genetics/52.3.643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  280. Yokota T., Gots J. S. Requirement of adenosine 3', 5'-cyclic phosphate for flagella formation in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1970 Aug;103(2):513–516. doi: 10.1128/jb.103.2.513-516.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  281. Young B. G., Hartman P. E. Sites of P22 and P221 prophage integration in Salmonella typhimurium. Virology. 1966 Feb;28(2):265–270. doi: 10.1016/0042-6822(66)90150-4. [DOI] [PubMed] [Google Scholar]
  282. Young B. G. Some phages released from P22-infected salmonella. Virology. 1966 Feb;28(2):249–264. doi: 10.1016/0042-6822(66)90149-8. [DOI] [PubMed] [Google Scholar]
  283. Yourno J. Composition and subunit structure of histidinol dehydrogenase from Salmonella typhimurium. J Biol Chem. 1968 Jun 25;243(12):3277–3288. [PubMed] [Google Scholar]
  284. Yourno J., Ino I. Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2. J Biol Chem. 1968 Jun 25;243(12):3273–3276. [PubMed] [Google Scholar]
  285. Yourno J., Kohno T., Roth J. R. Enzyme evolution: generation of a bifunctional enzyme by fusion of adjacent genes. Nature. 1970 Nov 28;228(5274):820–824. doi: 10.1038/228820a0. [DOI] [PubMed] [Google Scholar]
  286. Yourno J. Nature of the compensating frameshift in the double frameshift mutant hisD3018 R5 of Salmonella typhimurium. J Mol Biol. 1970 Mar;48(3):437–442. doi: 10.1016/0022-2836(70)90056-2. [DOI] [PubMed] [Google Scholar]
  287. Yourno J. Similarity of cross-suppressible frameshifts in Salmonella typhimurium. J Mol Biol. 1971 Nov 28;62(1):223–231. doi: 10.1016/0022-2836(71)90141-0. [DOI] [PubMed] [Google Scholar]
  288. Yuasa R., Levinthal M., Nikaido H. Biosynthesis of cell wall lipopolysaccharide in mutants of Salmonella. V. A mutant of Salmonella typhimurium defective in the synthesis of cytidine diphosphoabequose. J Bacteriol. 1969 Oct;100(1):433–444. doi: 10.1128/jb.100.1.433-444.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  289. ZINDER N. D. Hybrids of Escherichia and Salmonella. Science. 1960 Mar 18;131(3403):813–815. doi: 10.1126/science.131.3403.813. [DOI] [PubMed] [Google Scholar]
  290. ZINDER N. D., LEDERBERG J. Genetic exchange in Salmonella. J Bacteriol. 1952 Nov;64(5):679–699. doi: 10.1128/jb.64.5.679-699.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  291. ZINDER N. D. Sexuality and mating in salmonella. Science. 1960 Mar 25;131(3404):924–926. doi: 10.1126/science.131.3404.924. [DOI] [PubMed] [Google Scholar]
  292. Zarlengo M. H., Robinson G. W., Burns R. O. Threonine deaminase from Salmonella typhimurium. II. The subunit structure. J Biol Chem. 1968 Jan 10;243(1):186–191. [PubMed] [Google Scholar]

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