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. 1976 Jan;125(1):136–141. doi: 10.1128/jb.125.1.136-141.1976

Specific inhibition of phospholipid synthesis in plsA mutants of Escherichia coli.

T K Ray, J E Cronan Jr, G N Godson
PMCID: PMC233344  PMID: 173704

Abstract

plsA mutants of Escherichia coli are temperature-sensitive strains which possess two enzymes of abnormal thermolability, sn-glycerol 3-phosphate acyltransferase and adenylate kinase. Phospholipid synthesis is inhibited after shift of plsA mutants to temperatures at the lower end of the nonpermissive temperature range. This inhibition is not due to inactivation of the adenylate kinase activity since nucleic acid (and hence adenosine 5'-triphosphate) synthesis is inhibited only slightly. These results show that in vivo inactivation of the sn-glycerol 3-phosphate acyltransferase can be observed under conditions which allow normal adenylate kinase function.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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