| Literature DB >> 4576394 |
Abstract
The control of methionyl-transfer ribonucleic acid (tRNA) synthetase (l-methionine: soluble RNA ligase [adenosine monophosphate]) was studied in methionyl-tRNA synthetase mutants of Escherichia coli and Salmonella typhimurium. The results of activity determinations with crude extracts indicate that this enzyme of the E. coli mutant strain possessed a reduced affinity for methionine-tRNA, whereas this enzyme of the S. typhimurium mutant exhibited a decreased affinity for l-methionine. The differential rate of methionyl-tRNA synthetase formation in these two mutants was several-fold greater than that of the respective parental strains. On the other hand, the level of in vivo aminoacylation of methionine-tRNA was only about one-third that of the parent strains. These results suggest that aminoacylation of methionine-tRNA is a necessary step in repression control of methionyl-tRNA synthetase of both E. coli and S. typhimurium strains.Entities:
Mesh:
Substances:
Year: 1973 PMID: 4576394 PMCID: PMC285357 DOI: 10.1128/jb.114.3.1007-1013.1973
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490