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Title | Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 18, Issue 1, Page 6-13, Year 2011 |
Publish date | Dec 26, 2010 |
![]() | Bettina A Buschhorn / Georg Petzold / Marta Galova / Prakash Dube / Claudine Kraft / Franz Herzog / Holger Stark / Jan-Michael Peters / ![]() ![]() |
PubMed Abstract | 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. |
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Methods | EM (single particle) |
Resolution | 25.0 - 35.0 Å |
Structure data | ![]() EMDB-1820: ![]() EMDB-1821: ![]() EMDB-1822: |
Source |
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