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PMID: 378953 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. V. Mutants with increased levels of valyl-transfer ribonucleic acid synthetase.

Journal of bacteriology ·Vol. 139 ·No. 1 ·1979-07-00 ·Pages 165-75

Baer M, Low KB, Söll D

Abstract

Spontaneous revertants of a temperature-sensitive Escherichia coli strain harboring a thermolabile valyl-transfer ribonucleic acid (tRNA) synthetase were selected for growth at 40 degrees C. Of these, a large number still contain the thermolabile valyl-tRNA synthetase. Three of these revertants contained an increased level of the thermolabile enzyme. The genetic locus, valX, responsible for the enzyme overproduction, is adjacent to the structural gene, valS, of valyl-tRNA synthetase. Determination (by radioimmunoassay) of the turnover rates of valyl-tRNA synthetase showed that the increased level of valyl-tRNA synthetase is due to new enzyme synthesis rather than decreased rates of protein degradation.

MeSH Terms
Amino Acyl-tRNA Synthetases/biosynthesis,metabolism Bacterial Proteins/biosynthesis Escherichia coli/enzymology,genetics Genes, Regulator Mutation RNA, Bacterial/metabolism RNA, Transfer/metabolism Valine-tRNA Ligase/biosynthesis,genetics
Chemicals
Bacterial Proteins RNA, Bacterial RNA, Transfer Amino Acyl-tRNA Synthetases Valine-tRNA Ligase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Baer M
Low K B
Söll D
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32 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1979-07-00
Pages
165-75
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC216842
Subset
IM
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