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. 1970 Apr;102(1):193–203. doi: 10.1128/jb.102.1.193-203.1970

Isolation and Partial Characterization of Escherichia coli Mutants with Altered Glycyl Transfer Ribonucleic Acid Synthetases

William R Folk 1, Paul Berg 1
PMCID: PMC284986  PMID: 4908671

Abstract

Isolates with mutations in glyS, the structural gene for glycyl-transfer ribonucleic acid (tRNA) synthetase (GRS) in Escherichia coli, are frequently found among glycine auxotrophs. Extracts of glyS mutants have altered GRS activities. The mutants grow with normal growth rates in minimal media when high levels of glycine are provided. No other metabolite of a variety tested is capable of restoring normal growth. The glyS mutants fail to make ribonucleic acid (RNA) when depleted of exogenous glycine in strains which are RCstr but do so when the cells are RCrel. In contrast, biosynthetic mutants which are unable to synthesize glycine (glyA mutants) do not make RNA when deprived of glycine even if they are RCrel; in this case, RNA is synthesized upon glycine deprivation only when the nucleic acid precursors made from glycine are provided in the medium. The level of serine transhydroxymethylase is unaltered in extracts of any of the glyS mutants, even though the level of charged tRNAGly is at least 20-fold lower than that found in a prototrophic parent; this indicates that, if there is control over the synthesis of serine transhydroxymethylase, it is not modified by reduced levels of charging of the major species of tRNAGly.

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Selected References

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

  1. ALFOELDI L., STENT G. S., HOOGS M., HILL R. PHYSIOLOGICAL EFFECTS OF THE RNA CONTROL (RC) GENE IN E. COLI. Z Vererbungsl. 1963 Nov 21;94:285–302. doi: 10.1007/BF00894773. [DOI] [PubMed] [Google Scholar]
  2. ALFOLDI L., STENT G. S., CLOWES R. C. The chromosomal site of the RNA control (RC) locus in Escherichia coli. J Mol Biol. 1962 Sep;5:348–355. doi: 10.1016/s0022-2836(62)80077-1. [DOI] [PubMed] [Google Scholar]
  3. Böck A., Faiman L. E., Neidhardt F. C. Biochemical and genetic characterization of a mutant of Escherichia coli with a temperature-sensitive valyl ribonucleic acid synthetase. J Bacteriol. 1966 Oct;92(4):1076–1082. doi: 10.1128/jb.92.4.1076-1082.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Böck A., Neidhardt F. C. Location of the structural gene for glycyl ribonucleic acid synthetase by means of a strain of Escherichia coli possessing an unusual enzyme. Z Vererbungsl. 1966;98(3):187–192. doi: 10.1007/BF00888946. [DOI] [PubMed] [Google Scholar]
  5. Carbon J., Berg P., Yanofsky C. Missense suppression due to a genetically altered tRNA. Cold Spring Harb Symp Quant Biol. 1966;31:487–497. doi: 10.1101/sqb.1966.031.01.063. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Doolittle W. F., Yanofsky C. Mutants of Escherichia coli with an altered tryptophanyl-transfer ribonucleic acid synthetase. J Bacteriol. 1968 Apr;95(4):1283–1294. doi: 10.1128/jb.95.4.1283-1294.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. EIDLIC L., NEIDHARDT F. C. PROTEIN AND NUCLEIC ACID SYNTHESIS IN TWO MUTANTS OF ESCHERICHIA COLI WITH TEMPERATURE-SENSITIVE AMINOACYL RIBONUCLEIC ACID SYNTHETASES. J Bacteriol. 1965 Mar;89:706–711. doi: 10.1128/jb.89.3.706-711.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. EIDLIC L., NEIDHARDT F. C. ROLE OF VALYL-SRNA SYNTHETASE IN ENZYME REPRESSION. Proc Natl Acad Sci U S A. 1965 Mar;53:539–543. doi: 10.1073/pnas.53.3.539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Edlin G., Broda P. Physiology and genetics of the "ribonucleic acid control" locus in escherichia coli. Bacteriol Rev. 1968 Sep;32(3):206–226. doi: 10.1128/br.32.3.206-226.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. FANGMAN W. L., NEIDHARDT F. C. DEMONSTRATION OF AN ALTERED AMINOACYL RIBONUCLEIC ACID SYNTHETASE IN A MUTANT OF ESCHERICHIA COLI. J Biol Chem. 1964 Jun;239:1839–1843. [PubMed] [Google Scholar]
  12. Folk W. R., Berg P. Characterization of altered forms of glycyl transfer ribonucleic acid synthetase and the effects of such alterations on aminoacyl transfer ribonucleic acid synthesis in vivo. J Bacteriol. 1970 Apr;102(1):204–212. doi: 10.1128/jb.102.1.204-212.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. GORINI L., KAUFMAN H. Selecting bacterial mutants by the penicillin method. Science. 1960 Feb 26;131(3400):604–605. doi: 10.1126/science.131.3400.604. [DOI] [PubMed] [Google Scholar]
  14. Hill C. W., Foulds J., Soll L., Berg P. Instability of a missense suppressor resulting from a duplication of genetic material. J Mol Biol. 1969 Feb 14;39(3):563–581. doi: 10.1016/0022-2836(69)90146-6. [DOI] [PubMed] [Google Scholar]
  15. Hiraga S., Ito K., Hamada K., Yura T. A new regulatory gene for the tryptophan operon of Escherichia coli. Biochem Biophys Res Commun. 1967 Mar 9;26(5):522–527. doi: 10.1016/0006-291x(67)90095-2. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Kano Y., Matsushiro A., Shimura Y. Isolation of the novel regulatory mutants of the tryptophan biosynthetic system in Escherichia coli. Mol Gen Genet. 1968;102(1):15–26. doi: 10.1007/BF00341866. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. Neidhardt F. C. Roles of amino acid activating enzymes in cellular physiology. Bacteriol Rev. 1966 Dec;30(4):701–719. doi: 10.1128/br.30.4.701-719.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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]
  21. STACEY K. A., SIMSON E. IMPROVED METHOD FOR THE ISOLATION OF THYMINE-REQUIRING MUTANTS OF ESCHERICHIA COLI. J Bacteriol. 1965 Aug;90:554–555. doi: 10.1128/jb.90.2.554-555.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Schlesinger S., Nester E. W. Mutants of Escherichia coli with an altered tyrosyl-transfer ribonucleic acid synthetase. J Bacteriol. 1969 Oct;100(1):167–175. doi: 10.1128/jb.100.1.167-175.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Szentirmai A., Szentirmai M., Umbarger H. E. Isoleucine and valine metabolism of Escherichia coli. XV. Biochemical properties of mutants resistant to thiaisoleucine. J Bacteriol. 1968 May;95(5):1672–1679. doi: 10.1128/jb.95.5.1672-1679.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. 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]
  25. 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]
  26. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]

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