Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1

被引：79

作者：

Buschhorn, Bettina A. ^{[2
]}

Petzold, Georg ^{[2
]}

Galova, Marta ^{[2
]}

Dube, Prakash ^{[1
]}

Kraft, Claudine ^{[2
]}

Herzog, Franz ^{[2
]}

Stark, Holger ^{[1
,3
]}

Peters, Jan-Michael ^{[2
]}

机构：

[1] Max Planck Inst Biophys Chem, Gottingen, Germany

[2] Res Inst Mol Pathol, A-1030 Vienna, Austria

[3] Univ Gottingen, Dept Mol Electron Cryomicroscopy 3D, Inst Microbiol & Genet, Gottingen, Germany

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2011年 / 18卷 / 01期

基金：

奥地利科学基金会;

关键词：

ANAPHASE-PROMOTING COMPLEX; SPINDLE-ASSEMBLY CHECKPOINT; SACCHAROMYCES-CEREVISIAE; CRYSTAL-STRUCTURE; DESTRUCTION BOX; FLUORESCENT PROTEIN; DOC1/APC10; SUBUNIT; YEAST; COMPLEX/CYCLOSOME; RECOGNITION;

D O I：

10.1038/nsmb.1979

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 anaphase-promoting complex/cyclosome (APC/C) is a 22S ubiquitin ligase complex that initiates chromosome segregation and mitotic exit. We have used biochemical and electron microscopic analyses of Saccharomyces cerevisiae and human APC/C to address how the APC/C subunit Doc1 contributes to recruitment and processive ubiquitylation of APC/C substrates, and to understand how APC/C monomers interact to form a 36S dimeric form. We show that Doc1 interacts with Cdc27, Cdc16 and Apc1 and is located in the vicinity of the cullin-RING module Apc2-Apc11 in the inner cavity of the APC/C. Substrate proteins also bind in the inner cavity, in close proximity to Doc1 and the coactivator Cdh1, and induce conformational changes in Apc2-Apc11. Our results suggest that substrates are recruited to the APC/C by binding to a bipartite substrate receptor composed of a coactivator protein and Doc1.

引用

页码：6 / +

页数：9

共 37 条

[1] Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit [J].