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. 1970 Jul;103(1):178–183. doi: 10.1128/jb.103.1.178-183.1970

Mutants of Escherichia coli K-12 with an Altered Glutamyl-Transfer Ribonucleic Acid Synthetase

E J Murgola a,1, E A Adelberg a
PMCID: PMC248054  PMID: 4912521

Abstract

Three streptomycin-suppressible lethal mutants of Escherichia coli K-12 have been shown to possess structurally altered glutamyl-transfer ribonucleic acid (tRNA) synthetases. Each mutant synthetase displays a Km value for glutamate which is 10-fold higher than the parental value, and the mutations reside in two widely separate loci on the genetic map. Mixing of the mutant extracts in pairs gave no indication of in vitro complementation. All three enzymes charge the minor tRNAglu fraction identically, but one (EM 120) charges the major fraction at a twofold lower rate than do the other two (EM 102 and EM 111). Possible explanations for the existence of the two synthetase loci are presented.

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Selected References

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

  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. Freundlich M. Valyl-Transfer RNA: Role in Repression of the Isoleucine-Valine Enzymes in Escherichia coli. Science. 1967 Aug 18;157(3790):823–825. doi: 10.1126/science.157.3790.823-a. [DOI] [PubMed] [Google Scholar]
  6. GORINI L., KATAJA E. PHENOTYPIC REPAIR BY STREPTOMYCIN OF DEFECTIVE GENOTYPES IN E. COLI. Proc Natl Acad Sci U S A. 1964 Mar;51:487–493. doi: 10.1073/pnas.51.3.487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gillam I., Millward S., Blew D., von Tigerstrom M., Wimmer E., Tener G. M. The separation of soluble ribonucleic acids on benzoylated diethylaminoethylcellulose. Biochemistry. 1967 Oct;6(10):3043–3056. doi: 10.1021/bi00862a011. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. 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]
  10. Lazar M., Yaniv M., Gros F. Sur les propriétés d'une alanyl-t-RNA synthétase modifiée dans une souche d'Escherichia coli à croissance thermosensible. C R Acad Sci Hebd Seances Acad Sci D. 1968 Jan 29;266(5):531–534. [PubMed] [Google Scholar]
  11. Lee M. L., Muench K. H. Prolyl transfer ribonucleic acid synthetase of Escherichia coli. I. Purification and evidence for subunits. J Biol Chem. 1969 Jan 25;244(2):223–230. [PubMed] [Google Scholar]
  12. Lengyel P., Söll D. Mechanism of protein biosynthesis. Bacteriol Rev. 1969 Jun;33(2):264–301. doi: 10.1128/br.33.2.264-301.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lennarz W. J., Nesbitt J. A., 3rd, Reiss J. The participation of sRNA in the enzymatic synthesis of O-L-lysyl phosphatidylgylcerol in Staphylococcus aureus. Proc Natl Acad Sci U S A. 1966 Apr;55(4):934–941. doi: 10.1073/pnas.55.4.934. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lindahl T., Adams A., Fresco J. R. Renaturation of transfer ribonucleic acids through site binding of magnesium. Proc Natl Acad Sci U S A. 1966 Apr;55(4):941–948. doi: 10.1073/pnas.55.4.941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Malcolm N. L. Subunit structure and function of Micrococcus cryophilus glutamyl transfer RNA synthetase. Biochim Biophys Acta. 1969 Oct 22;190(2):347–357. doi: 10.1016/0005-2787(69)90085-9. [DOI] [PubMed] [Google Scholar]
  16. Marcus M., Halpern Y. S. Genetic analysis of the glutamate permease in Escherichia coli K-12. J Bacteriol. 1969 Mar;97(3):1118–1128. doi: 10.1128/jb.97.3.1118-1128.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Murgola E. J., Adelberg E. A. Streptomycin-suppressible lethal mutations in Escherichia coli. J Bacteriol. 1970 Jul;103(1):20–26. doi: 10.1128/jb.103.1.20-26.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Nass G. Regulation of histidine biosynthetic enzymes in a mutant of Escherichia coli with an altered histidyl-tRNA synthetase. Mol Gen Genet. 1967;100(2):216–224. doi: 10.1007/BF00333608. [DOI] [PubMed] [Google Scholar]
  19. Neidhardt F. C., Marchin G. L., McClain W. H., Boyd R. F., Earhart C. F. Phage-induced modification of valyl-tRNA synthetase. J Cell Physiol. 1969 Oct;74(2 Suppl):87+–87+. doi: 10.1002/jcp.1040740408. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. Preddie E. C. Tryptophanyl transfer ribonucleic acid synthetase from bovine pancreas. II. The chemically different subunits. J Biol Chem. 1969 Jul 25;244(14):3958–3968. [PubMed] [Google Scholar]
  22. RAVEL J. M., WANG S. F., HEINEMEYER C., SHIVE W. GLUTAMYL AND GLUTAMINYL RIBONUCLEIC ACID SYNTHETASES OF ESCHERICHIA COLI W. SEPARATION, PROPERTIES, AND STIMULATION OF ADENOSINE TRIPHOSPHATE-PYROPHOSPHATE EXCHANGE BY ACCEPTOR RIBONUCLEIC ACID. J Biol Chem. 1965 Jan;240:432–438. [PubMed] [Google Scholar]
  23. Ray D. K., Rappaport H. P. Further investigations of the multiple fractions of leucyl transfer ribonucleic acid synthetase activity from Escherichia coli. Biochim Biophys Acta. 1970 Jan 21;199(1):79–85. doi: 10.1016/0005-2787(70)90696-9. [DOI] [PubMed] [Google Scholar]
  24. 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]
  25. Roy K. L., Söll D. Purification of five serine transfer ribonucleic acid species from Escherichia coli and their acylation by homologous and heterologous seryl transfer ribonucleic acid synthetases. J Biol Chem. 1970 Mar 25;245(6):1394–1400. [PubMed] [Google Scholar]
  26. 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]
  27. 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]
  28. 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]
  29. 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]
  30. 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]
  31. Wilcox M., Nirenberg M. Transfer RNA as a cofactor coupling amino acid synthesis with that of protein. Proc Natl Acad Sci U S A. 1968 Sep;61(1):229–236. doi: 10.1073/pnas.61.1.229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Yaniv M., Gros F. Studies on valyl-tRNA synthetase and tRNA from Escherichia coli. 3. Valyl-tRNA synthetases from thermosensitive mutants of Escherichia coli. J Mol Biol. 1969 Aug 28;44(1):31–45. doi: 10.1016/0022-2836(69)90403-3. [DOI] [PubMed] [Google Scholar]
  33. Yaniv M., Jacob F., Gros F. Mutations thermosensibles des systèmes activant la valine chez E. coli. Bull Soc Chim Biol (Paris) 1965;47(8):1609–1626. [PubMed] [Google Scholar]
  34. Yu C. T., Rappaport H. P. Multiple fractions of leucyl-transfer ribonucleic acid synthetase activity from Escherichia coli. Biochim Biophys Acta. 1966 Jul 20;123(1):134–141. doi: 10.1016/0005-2787(66)90166-3. [DOI] [PubMed] [Google Scholar]

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