The F1F0-ATPase of Escherichia coli. The substitution of alanine by threonine at position 25 in the c-subunit affects function but not assembly

Anthony L. Fimmel, David A. Jans, Lyndall Hatch, Lewis B. James, Frank Gibson, Graeme B. Cox

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17 Citations (Scopus)

Abstract

A mutant strain of Escherichia coli carrying a mutation in the uncE gene which codes for the c-subunit of the F1F0-ATPase has been isolated and examined. The mutant allele, designated uncE513, results in alanine at position 25 of the c-subunit being replaced by threonine. The mutant F1F0-ATPase appears to be fully assembled and is partially functional with respect to oxidative phosphorylation. The ATPase activity of membranes from the mutant strain is resistant to the inhibitor dicyclohexylcarbodiimide, but this is due to the F1-ATPase being lost from the membranes in the presence of the inhibitor. Mutant membranes from which the F1-ATPase has been removed have a greatly reduced proton permeability compared with similarly treated normal membranes. The results are discussed in relation to a previously proposed mechanism of oxidative phosphorylation.

Original languageEnglish
Pages (from-to)252-258
Number of pages7
JournalBBA - Bioenergetics
Volume808
Issue number2
DOIs
Publication statusPublished - 17 Jul 1985
Externally publishedYes

Keywords

  • (E. coli)
  • Amino acid substitution
  • FF-ATPase
  • Oxidative phosphorylation

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