Identification of an uncoupling mutation affecting the b subunit of F1F0 ATP synthase in Escherichia coli

Tamara L. Caviston, Christian J. Ketchum, Paul L. Sorgen, Robert K. Nakamoto, Brian D. Cain

Research output: Contribution to journalArticle

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Abstract

A specific b subunit arginine, b(Arg-36) in Escherichia coli, displays evolutionary conservation among bacterial F1F0 ATP synthases. Site- directed mutagenesis was used to generate a collection of mutations affecting b(Arg-36). The phenotype differed depending upon the substitution, and the b(Arg-36→Glu) and b(Arg-36→Ile) substitutions virtually abolished enzyme function. Although the total amounts of F1F0 ATP synthase present in the membranes prepared from mutant strains were reduced, the primary effect of the b(Arg-36) substitutions was on the activities of the intact enzyme complexes. The most interesting result was that the b(Arg-36-Glu) substitution results in the uncoupling of a functional F0 from F1 ATP hydrolysis activity.

Original languageEnglish (US)
Pages (from-to)201-206
Number of pages6
JournalFEBS Letters
Volume429
Issue number2
DOIs
Publication statusPublished - Jun 12 1998

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Keywords

  • FF ATP synthase
  • Proton translocation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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