Affiliation:
1. Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan 48201
Abstract
ABSTRACT
Expression of the genes for the membrane-bound F
o
sector of the
Escherichia coli
F
1
F
o
proton-translocating ATPase can respond to changes in metabolic conditions, and these changes are reflected in alterations in the subunit stoichiometry of the oligomeric F
o
proton channel. Transcriptional and translational
lacZ
fusions to the promoter and to two F
o
genes show that, during growth on the nonfermentable carbon source succinate, transcription of the operon and translation of
uncB
, encoding the a subunit of F
o
, are higher than during growth on glucose. In contrast, translation of the
uncE
gene, encoding the c subunit of F
o
, is higher during growth on glucose than during growth on succinate. Translation rates of both
uncB
and
uncE
change as culture density increases, but transcription rates do not. Quantitation of the c stoichiometry shows that more c subunits are assembled into the F
1
F
o
ATPase in cells grown on glucose than in cells grown on succinate.
E. coli
therefore appears to have a mechanism for regulating the composition and, presumably, the function of the ATPase in response to metabolic circumstances.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology