Evidence for energy-dependent transposition of core lipopolysaccharide across the inner membrane of Salmonella typhimurium

B. C. McGrath, M. J. Osborn

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

The uncoupler 2,4-dinitrophenol blocks the final step of lipopolysaccharide assembly-transfer of O antigen from undecaprenyl pyrophosphate to core lipopolysaccharide - in intact Salmonella typhimurium but not in isolated membrane fractions. The O-antigen ligase enzyme is not inhibited by dinitrophenol in vitro, and core lipopolysaccharide synthesized in the presence of uncoupler in vivo is functional as acceptor of O antigen in vitro. The evidence strongly suggests that maintenance of proton motive force is required for transmembrane transposition of core lipopolysaccharide to the active site of O-antigen ligase at the periplasmic face of the inner membrane.

Original languageEnglish (US)
Pages (from-to)3134-3137
Number of pages4
JournalJournal of bacteriology
Volume173
Issue number10
DOIs
StatePublished - 1991

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

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