ASSEMBLY OF THE ESCHERICHIA-COLI F1F0 ATPASE, A LARGE MULTIMERIC MEMBRANE-BOUND ENZYME

被引：18
|
作者：
BRUSILOW, WSA
机构：
[1] Department of Biochemistry, Wayne State University School of Medicine, Detroit, Michigan, 48201
来源：
MOLECULAR MICROBIOLOGY | 1993年 / 9卷 / 03期
关键词：
D O I：
10.1111/j.1365-2958.1993.tb01703.x
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The F1F0 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 F1. subunits on the assembly and proton permeability of the F0 proton channel, and the possible advantages to assembly of the particular arrangement of genes in the unc operon.
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页码：419 / 424
页数：6
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