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 Lettjournal_title
FEBS lettersauthors
Caviston TL,Ketchum CJ,Sorgen PL,Nakamoto RK,Cain BDdoi
10.1016/s0014-5793(98)00597-3subject
Has Abstractpub_date
1998-06-12 00:00:00pages
201-6issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00597-3journal_volume
429pub_type
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