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Assembly of the Escherichia coli F 1 F 0 ATPase, a large multimeric membrane‐bound enzyme
Author(s) -
Brusilow William S. A.
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01703.x
Subject(s) - operon , biology , escherichia coli , atpase , biochemistry , enzyme , membrane , biophysics , gene
Summary The F 1 F 0 proton translocating ATPase of Escherichia coli is a large membrane‐bound enzyme complex consisting of more than 20 polypeptides that are encoded by the unc operon. Besides being a system for analysing the enzymology of ATP synthesis and energy coupling, the ATPase is a model system for determining how large oligomeric membrane‐bound proteins are synthesized and assembled. The assembly of the ATPase involves differential gene expression and assembly of the subunits within the membrane and with each other. This review discusses the influence of F 1 subunits on the assembly and proton permeability of the F 0 proton channel, and the possible advantages to assembly of the particular arrangement of genes in the unc operon.