Abstract
A cold-sensitive mutant of Salmonella typhimurium LT2 that grows at 37 C but not at 20 C has altered repression regulation in at least two amino acid biosynthetic pathways (histidine and isoleucine). The lesion conferring cold sensitivity that is linked with hisW is recessive. Assays for the acceptance of some amino acids by transfer ribonucleic acid (tRNA) reveal a decreased ability of the mutant tRNA to accept arginine, phenylalanine, and histidine. A mutation in a gene for tRNA maturation is a likely possibility for the mutation producing these effects on growth, regulation, and amino acid acceptance.
Full text
PDF








Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- AMES B. N., HARTMAN P. E., JACOB F. Chromosomal alterations affecting the regulation of histidine biosynthetic enzymes in Salmonella. J Mol Biol. 1963 Jul;7:23–42. doi: 10.1016/s0022-2836(63)80016-9. [DOI] [PubMed] [Google Scholar]
- 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]
- Abd-el-Al A., Ingraham J. L. Control of carbamyl phosphate synthesis in Salmonella typhimurium. J Biol Chem. 1969 Aug 10;244(15):4033–4038. [PubMed] [Google Scholar]
- Brenner M., Ames B. N. Histidine regulation in Salmonella typhimurium. IX. Histidine transfer ribonucleic acid of the regulatory mutants. J Biol Chem. 1972 Feb 25;247(4):1080–1088. [PubMed] [Google Scholar]
- 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]
- Condon S., Ingraham J. L. Cold-sensitive mutation of Pseudomonas putida affecting enzyme synthesis at low temperature. J Bacteriol. 1967 Dec;94(6):1970–1981. doi: 10.1128/jb.94.6.1970-1981.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dempsey W. B. 3-Phosphoserine transaminase mutants of Escherichia coli B. J Bacteriol. 1969 Nov;100(2):1114–1115. doi: 10.1128/jb.100.2.1114-1115.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Guthrie C., Nashimoto H., Nomura M. Structure and function of E. coli ribosomes. 8. Cold-sensitive mutants defective in ribosome assembly. Proc Natl Acad Sci U S A. 1969 Jun;63(2):384–391. doi: 10.1073/pnas.63.2.384. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HARTMAN P. E., HARTMAN Z., SERMAN D. Complementation mapping by abortive transduction of histidine requiring Salmonella mutants. J Gen Microbiol. 1960 Apr;22:354–368. doi: 10.1099/00221287-22-2-354. [DOI] [PubMed] [Google Scholar]
- Hirshfield I. N., Horn P. C., Hopwood D. A., Maas W. K., DeDeken R. Studies on the mechanism of repression of arginine biosynthesis in Escherichia coli. 3. Repression of enzymes of arginine biosynthesis in arginyl-tRNA synthetase mutants. J Mol Biol. 1968 Jul 14;35(1):83–93. doi: 10.1016/s0022-2836(68)80038-5. [DOI] [PubMed] [Google Scholar]
- Hoffmann B., Ingraham J. L. A cold-sensitive mutant of Salmonella typhimurium which requires tryptophan for growth at 20 degrees. Biochim Biophys Acta. 1970 Feb 24;201(2):300–308. doi: 10.1016/0304-4165(70)90304-1. [DOI] [PubMed] [Google Scholar]
- 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]
- Katz L. Selection of araB and araC mutants of Escherichia coli B-r by resistance to ribitol. J Bacteriol. 1970 May;102(2):593–595. doi: 10.1128/jb.102.2.593-595.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- 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]
- MONOD J., COHEN-BAZIRE G., COHN M. Sur la biosynthèse de la beta-galactosidase (lactase) chez Escherichia coli; la spécificité de l'induction. Biochim Biophys Acta. 1951 Nov;7(4):585–599. doi: 10.1016/0006-3002(51)90072-8. [DOI] [PubMed] [Google Scholar]
- Ning C., Gest H. Regulation of L-isoleucine biosynthesis in the photosynthetic bacterium rhodospirillum rubrum. Proc Natl Acad Sci U S A. 1966 Dec;56(6):1823–1827. doi: 10.1073/pnas.56.6.1823. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Donovan G. A., Ingraham J. L. Cold-sensitive mutants of Escherichia coli resulting from increased feedback inhibition. Proc Natl Acad Sci U S A. 1965 Aug;54(2):451–457. doi: 10.1073/pnas.54.2.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Roth J. R., Ames B. N. Histidine regulatory mutants in Salmonella typhimurium II. Histidine regulatory mutants having altered histidyl-tRNA synthetase. J Mol Biol. 1966 Dec 28;22(2):325–333. doi: 10.1016/0022-2836(66)90135-5. [DOI] [PubMed] [Google Scholar]
- 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]
- SCHLESINGER S., MAGASANIK B. EFFECT OF ALPHA-METHYLHISTIDINE ON THE CONTROL OF HISTIDINE SYNTHESIS. J Mol Biol. 1964 Sep;9:670–682. doi: 10.1016/s0022-2836(64)80174-1. [DOI] [PubMed] [Google Scholar]
- 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]
- 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]
- 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]
- Smith H. O., Levine M. A phage P22 gene controlling integration of prophage. Virology. 1967 Feb;31(2):207–216. doi: 10.1016/0042-6822(67)90164-x. [DOI] [PubMed] [Google Scholar]
- 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]
- Tessman I. Mutagenic treatment of double- and single-stranded DNA phages T4 ans S13 with hydroxylamine. Virology. 1968 Jun;35(2):330–333. doi: 10.1016/0042-6822(68)90275-4. [DOI] [PubMed] [Google Scholar]