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PMID: 340903 Published · ppublish English Journal Article

Suppression of a defective alanyl-tRNA synthetase in Escherichia coli: a compensatory mutation to high alanine affinity.

Molecular & general genetics : MGG ·Vol. 156 ·No. 2 ·1977-11-14 ·Pages 221-7

Theall G, Low KB, Söll D

Abstract

Among temperature resistant revertants of a temperature sensitive E. Coli alanyl-tRNA synthetase mutant a strain was found which contains an alanyl-tRNA synthetase with an additional mutation in the structural gene of the enzyme. This mutant enzyme has a 9 or 38 fold decreased Km value for alanine compared to that of the thermolabile parental enzyme or to wild-type enzyme, respectively. The alaS gene maps just counterclockwise from recA on the E. coli map (94% cotransduction frequency). It appears that the enzyme's increased affinity for alanine is the mechanism of suppressing the temperature sensitive character of the cell. In addition, some cold-sensitive temperature resistant revertants were found, where the cold-sensitive character mapped near strA. Presumably they are due to changes in ribosomal proteins as characterized by Ruffler et al. (1974).

MeSH Terms
Alanine/metabolism Alanine-tRNA Ligase/metabolism Amino Acids/metabolism Amino Acyl-tRNA Synthetases/metabolism Bacterial Proteins/biosynthesis Escherichia coli/enzymology,genetics Genes Hot Temperature Kinetics Mutation Suppression, Genetic
Chemicals
Amino Acids Bacterial Proteins Amino Acyl-tRNA Synthetases Alanine-tRNA Ligase Alanine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Theall G
Low K B
Söll D
References (19)
19 references, click to expand
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Article Info
Journal
Molecular & general genetics : MGG
Abbr.
Mol Gen Genet
ISSN
0026-8925
DOI
10.1007/BF00283495
Published
1977-11-14
Pages
221-7
Language
English
Region
Germany
NLM ID
0125036
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00283495
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