Specific inhibition of phospholipid synthesis in plsA mutants of Escherichia coli

T. K. Ray, John E Cronan, G. N. Godson

Research output: Contribution to journalArticlepeer-review

Abstract

plsA mutants of E. 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 nonpermisive temperature range. This inhibition is not due to inactivation of the adenylate kinase activity since nucleic acid (and hence adenosine 5' triphosphate) synthesis in 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.

Original languageEnglish (US)
Pages (from-to)136-141
Number of pages6
JournalJournal of Bacteriology
Volume125
Issue number1
StatePublished - 1976
Externally publishedYes

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

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