Home LiteratureArticle Details
PMID: 1092645 Published · ppublish English Journal Article

Thermosensitive mutants of Escherichia coli K-12 altered in the catalytic Subunit and in a Regulatory factor of the glutamy-transfer ribonucleic acid synthetase.

Journal of bacteriology ·Vol. 122 ·No. 2 ·1975-05-00 ·Pages 352-8

Lapointe J, Delcuve G

Abstract

The glutamyl-transfer ribonucleic acid synthetase (GluRS) of a partial revertants (ts plus or minus) of the thermosensitive (ts) mutant strain JP1449 (LOcus gltx) and of a ts mutant strain EM111-ts1 with a lesion in or near the locus gltx have been studied to find the relation between these two genetic loci known to influence the GluRS activity in vitro and the presence of a catalytic subunit and of a regulatory subunit in the GluRS purified from Escherichia coli K-12. The ts character of strain JP1449-18ts plus or minus is co-transduced with the marker dsdA at the same frequency as is the ts character of strain JP1449. Its purified GluRS is very thermolabile and its Km for glutamate is higher than that of a wild-type GluRS. These results indicate that the locus gltX is in the structural gene for the catalytic subunit of this enzyme. The location of the mutation causing the partial ts reversion in strain JP1449-18ts plus or minus is discussed. The GluRS purified from the ts mutant strain EM111-ts1 has the same stability as the wild-type enzyme, but its Km forglutamate increases with the temperature, suggesting that the locus gltE codes for a regulatory factor, possibly for the polypeptide chain that is co-purified with the catalytic subunit.

MeSH Terms
Acylation Amino Acyl-tRNA Synthetases/biosynthesis Cell-Free System Chromosome Mapping Escherichia coli/enzymology Genes, Regulator Glutamate-tRNA Ligase/biosynthesis,metabolism Glutamates/metabolism Mutation Surface-Active Agents Temperature Transduction, Genetic
Chemicals
Glutamates Surface-Active Agents Amino Acyl-tRNA Synthetases Glutamate-tRNA Ligase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lapointe J
Delcuve G
References (23)
23 references, click to expand
  1. RNA overproducing revertants of an alanyl-tRNA synthetase mutant of Escherichia coli.
    Mol Gen Genet. 1972;119(4):323-35 PMID: 4567806
  2. Evidence for the existence of two arginyl-transfer ribonucleic acid synthetase activities in Escherichia coli.
    J Bacteriol. 1973 Feb;113(2):891-4 PMID: 4570610
  3. Mapping of the d-serine deaminase region in Escherichia coli K-12.
    Genetics. 1967 Jan;55(1):91-9 PMID: 5340178
  4. Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme.
    Eur J Biochem. 1971 May 28;20(2):283-300 PMID: 4934682
  5. 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):204-12 PMID: 4908672
  6. Further evidence for a single leucyl transfer ribonucleic acid synthetase capable of charging five leucine transfer ribonucleic acids in Escherichia coli.
    J Biol Chem. 1971 Apr 10;246(7):2207-10 PMID: 4324563
  7. Two enzymatically active forms of lysyl-tRNA synthetase from E. coli B.
    FEBS Lett. 1972 May 1;22(2):231-234 PMID: 11946604
  8. Mutants of Escherichia coli unable to make protein at 42 C.
    J Bacteriol. 1971 Nov;108(2):790-8 PMID: 4942764
  9. Lysis of Escherichia coli with a neutral detergent.
    Biochim Biophys Acta. 1967 Dec 19;149(2):476-88 PMID: 4966087
  10. Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. I. Purification and properties.
    J Biol Chem. 1972 Aug 25;247(16):4966-74 PMID: 4341531
  11. Transduction of linked genetic characters of the host by bacteriophage P1.
    Virology. 1955 Jul;1(2):190-206 PMID: 13267987
  12. Isolation and characterization of a regulatory mutant of an aminoacyl-transfer ribonucleic acid synthetase in Escherichia coli K-12.
    J Bacteriol. 1973 Mar;113(3):1096-103 PMID: 4570769
  13. Thermosensitive mutants of Escherichia coli unable to propagate RNA phage at 42 degrees C and altered in protein synthesis.
    Eur J Biochem. 1974 Apr 16;43(3):583-90 PMID: 4598753
  14. Selection of temperature-sensitive activating enzyme mutants in Escherichia coli.
    J Bacteriol. 1968 Mar;95(3):991-7 PMID: 4868365
  15. Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. 3. Influence of the 46K protein on the affinity of the 56K glutamyl transfer ribonucleic acid synthetase for its substrates.
    J Biol Chem. 1972 Aug 25;247(16):4982-5 PMID: 4560497
  16. DEMONSTRATION OF AN ALTERED AMINOACYL RIBONUCLEIC ACID SYNTHETASE IN A MUTANT OF ESCHERICHIA COLI.
    J Biol Chem. 1964 Jun;239:1839-43 PMID: 14213362
  17. Aminoacyl-tRNA synthetases: sone recent results and achievements.
    Adv Enzymol Relat Areas Mol Biol. 1974;40(0):141-238 PMID: 4365538
  18. PHENOTYPIC REPAIR BY STREPTOMYCIN OF DEFECTIVE GENOTYPES IN E. COLI.
    Proc Natl Acad Sci U S A. 1964 Mar;51:487-93 PMID: 14171463
  19. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  20. Leucyl-tRNA synthetase. Two forms of the enzyme: relation between structural and catalytic properties.
    Eur J Biochem. 1971 Dec 10;23(3):459-67 PMID: 4945111
  21. Mutants of Escherichia coli K-12 with an altered glutamyl-transfer ribonucleic acid synthetase.
    J Bacteriol. 1970 Jul;103(1):178-83 PMID: 4912521
  22. Temperature-sensitive osmotic remedial mutants of Escherichia coli.
    J Bacteriol. 1972 Nov;112(2):661-5 PMID: 4563969
  23. Linkage map of Escherichia coli strain K-12.
    Bacteriol Rev. 1972 Dec;36(4):504-24 PMID: 4568762
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1975-05-00
Pages
352-8
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC246064
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]