ATP-Dependent Proteases in Bacteria

被引:37
|
作者
Bittner, Lisa-Marie [1 ]
Arends, Jan [1 ]
Narberhaus, Franz [1 ]
机构
[1] Ruhr Univ Bochum, Microbial Biol, Bochum, Germany
关键词
AAA protein; ATPase; protease; AAA PLUS PROTEASE; ESCHERICHIA-COLI LON; REPLICATIVE HEXAMERIC HELICASE; TRANSCRIPTION ACTIVATOR SOXS; ZINC-BINDING DOMAIN; CRYSTAL-STRUCTURE; PROTEOLYTIC MACHINE; SUBSTRATE DEGRADATION; CLPAP PROTEASE; POLYPEPTIDE TRANSLOCATION;
D O I
10.1002/bip.22831
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
AAA 1 proteases are universal barrel-like and ATP-fueled machines preventing the accumulation of aberrant proteins and regulating the proteome according to the cellular demand. They are characterized by two separate operating units, the ATPase and peptidase domains. ATP-dependent unfolding and translocation of a substrate into the proteolytic chamber is followed by ATP-independent degradation. This review addresses the structure and function of bacterial AAA 1 proteases with a focus on the ATP-driven mechanisms and the coordinated movements in the complex mainly based on the knowledge of ClpXP. We conclude by discussing strategies how novel protease substrates can be trapped by mutated AAA 1 protease variants. (C) 2016 Wiley Periodicals, Inc.
引用
收藏
页码:505 / 517
页数:13
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