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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Caviston TL,Ketchum CJ,Sorgen PL,Nakamoto RK,Cain BD

doi

10.1016/s0014-5793(98)00597-3

subject

Has Abstract

pub_date

1998-06-12 00:00:00

pages

201-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00597-3

journal_volume

429

pub_type

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