期刊
EMBO REPORTS
卷 9, 期 12, 页码 1237-1243出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/embor.2008.190
关键词
Blm10; proteasome; open gate; quality control
资金
- Deutsche Forschungsgemeinschaft [301/4-1]
Blm10, a crucial protease of eukaryotic cells, is bound to yeast proteasome core particles (CPs). Two gates, at both ends of the CP, control the access of protein substrates to the catalytic cavity of the CP. Normally, substrate access is auto-inhibited by a closed gate conformation unless regulatory complexes are bound to the CP and translocate protein substrates in an ATP-dependent manner. Here, we provide evidence that Blm10 recognizes preactivated open gate CPs, which are assumed to exist in an equilibrium with inactive closed gate CP. Consequently, single-capped Blm10-CP shows peptide hydrolysis activity. Under conditions of disturbed CP assembly, as well as in open gate mutants, pre-activated CP or constitutively active CP, respectively, prevail. Then, Blm10 sequesters disordered and open gate CP by forming double-capped Blm102-CP in which peptide hydrolysis activity is repressed. We conclude that Blm10 distinguishes between gate conformations and regulates the activation of CP.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据