| Literature DB >> 8152 |
E Boy, F Reinisch, C Richaud, J C Patte.
Abstract
A mutant of lysyl-tRNA synthetase has been isolated in Escherichia coli K12. With this strain the Kmapp for lysine is 25 fold higher than with the parental strain. The percentage of charged tRNAlys in vivo is only 7 per cent (as against 65 per cent with HFR H). Under these conditions no derepression of synthesis is observed for three lysine biosynthetic enzymes (AK III, ASA-dehydrogenase, DAP-decarboxylase) ; a partial derepression is obtained in the case of the dhdp-reductase. Thus lysyl-tRNA does not act as the only corepressor molecule in the lysine regulon.Entities:
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Year: 1976 PMID: 8152 DOI: 10.1016/s0300-9084(76)80372-0
Source DB: PubMed Journal: Biochimie ISSN: 0300-9084 Impact factor: 4.079