Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly
Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly
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DOI：
10.1093/embo-reports/kve203
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发表时间：
2001-10-01
期刊：
影响因子：
7.7
通讯作者：
Madura, K
中科院分区：
文献类型：
--
作者：
Chen, L;Shinde, U;Madura, K
Rad23 是一种 DNA 修复蛋白，可促进核苷酸切除修复复合物的组装。 Rad23 可以通过 N 端泛素样结构域与 26S 蛋白酶体相互作用，并在体外和体内抑制底物连接的多泛素 (multi-Ub) 链的组装。值得注意的是，Rad23 可以结合与一些泛素 (Ub) 部分缀合的蛋白水解底物。我们在此报告，Rad23 中的两个泛素相关 (UBA) 结构域与 Ub 形成非共价相互作用。缺乏任一 UBA 序列的突变体能够阻断底物连接的多 Ub 链的组装，尽管缺乏两个 UBA 结构域的突变体受到显着损害。这些研究表明，Rad23 活性需要与 Ub 相互作用，并且其他含有 UBA 的蛋白质可能具有类似的功能。
Rad23 is a DNA repair protein that promotes the assembly of the nucleotide excision repair complex. Rad23 can interact with the 26S proteasome through an N-terminal ubiquitin-like domain, and inhibits the assembly of substrate-linked multiubiquitin (multi-Ub) chains in vitro and in vivo. Significantly, Rad23 can bind a proteolytic substrate that is conjugated to a few ubiquitin (Ub) moieties. We report here that two ubiquitin-associated (UBA) domains in Rad23 form non-covalent interactions with Ub. A mutant that lacked either UBA sequence was capable of blocking the assembly of substrate-linked multi-Ub chains, although a mutant that lacked both UBA domains was significantly impaired. These studies suggest that the interaction with Ub is required for Rad23 activity and that other UBA-containing proteins may have a similar function.