ClpP: A distinctive family of cylindrical energy-dependent serine proteases

被引：178

作者：

Yu, Angela Yeou Hsiung ^{[1
]}

Houry, Walid A. ^{[1
]}

机构：

[1] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada

来源：

FEBS LETTERS | 2007年 / 581卷 / 19期

关键词：

C1pP; cylindrical protease; serine protease; C1pR; AAA plus chaperone;

D O I：

10.1016/j.febslet.2007.04.076

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：

Processes maintaining protein homeostasis in the cell are governed by the activities of molecular chaperones that mainly assist in the folding of polypeptide chains and by a large class of proteases that regulate protein levels through degradation. ClpP proteases; define a distinctive family of cylindrical, energy-dependent serine proteases that are highly conserved throughout bacteria and eukaryota. They typically interact with ATP-dependent AAA+ chaperones; that bind and unfold target substrates and then translocate them into ClpP for degradation. Structural and functional studies have provided a detailed view of the mechanism of function of this class of proteases. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3749 / 3757

页数：9

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