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-Structure paper
タイトル | Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 18, Issue 1, Page 6-13, Year 2011 |
掲載日 | 2010年12月26日 |
著者 | Bettina A Buschhorn / Georg Petzold / Marta Galova / Prakash Dube / Claudine Kraft / Franz Herzog / Holger Stark / Jan-Michael Peters / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Struct Mol Biol / PubMed:21186364 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 25.0 - 35.0 Å |
構造データ | EMDB-1820: EMDB-1821: EMDB-1822: |
由来 |
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