Defining how ubiquitin receptors hHR23a and S5a bind polyubiquitin
Defining how ubiquitin receptors hHR23a and S5a bind polyubiquitin
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DOI：
10.1016/j.jmb.2007.03.008
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发表时间：
2007-05-25
影响因子：
5.6
通讯作者：
Walters, Kylie J.
中科院分区：
文献类型：
--
作者：
Kang, Yang;Chen, Xiang;Walters, Kylie J.
泛素受体将底物泛素化与蛋白酶体降解联系起来。HHR 23 a通过也结合泛素的表面结合蛋白酶体亚基5a（S5a）。我们报告说，UIM2的S5a优先结合hHR23a的多聚泛素，我们提供了一个模型的三元复合物，我们预计代表的机制之一，所使用的蛋白酶体捕获泛素化底物。此外，我们证明，hHR23 a是令人惊讶的善于螯合的多聚泛素链的泛素部分，并提供证据表明，它和泛素化的底物是致力于彼此结合后。(c)2007爱思唯尔有限公司保留所有权利。
Ubiquitin receptors connect substrate ubiquitylation to proteasomal degradation. HHR23a binds proteasome subunit 5a (S5a) through a surface that also binds ubiquitin. We report that UIM2 of S5a binds preferentially to hHR23a over polyubiquitin, and we provide a model for the ternary complex that we expect represents one of the mechanisms used by the proteasome to capture ubiquitylated substrates. Furthermore, we demonstrate that hHR23a is surprisingly adept at sequestering the ubiquitin moieties of a polyubiquitin chain, and provide evidence that it and the ubiquitylated substrate are committed to each other after binding. (c) 2007 Elsevier Ltd. All rights reserved.