...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular cell >OTUB1 Co-opts Lys48-Linked Ubiquitin Recognition to Suppress E2 Enzyme Function
【24h】

OTUB1 Co-opts Lys48-Linked Ubiquitin Recognition to Suppress E2 Enzyme Function

机译：OTUB1选择Lys48连接的泛素识别来抑制E2酶功能

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Ubiquitylation entails the concerted action of E1, E2, and E3 enzymes. We recently reported that OTUB1, a deubiquitylase, inhibits the DNA damage response independently of its isopeptidase activity. OTUB1 does so by blocking ubiquitin transfer by UBC13, the cognate E2 enzyme for RNF168. OTUB1 also inhibits E2s of the UBE2D and UBE2E families. Herewe elucidate the structural mechanism by which OTUB1 binds E2s to inhibit ubiquitin transfer. OTUB1 recognizes ubiquitin-charged E2s through contacts with both donor ubiquitin and the E2 enzyme. Surprisingly, free ubiquitin associates with the canonical distal ubiquitin-binding site on OTUB1 to promote formation of the inhibited E2 complex. Lys48 of donor ubiquitin lies near the OTUB1 catalytic site and the C terminus of free ubiquitin, a configuration that mimics the products of Lys48-linked ubiquitin chain cleavage. OTUB1 therefore co-opts Lys48-linked ubiquitin chain recognition to suppress ubiquitin conjugation and the DNA damage response.
机译：泛素化需要E1，E2和E3酶的协同作用。我们最近报道了OTUB1，一种去泛素化酶，独立于其异肽酶活性抑制DNA损伤反应。 OTUB1通过阻止UBC13（RNF168的同源E2酶）阻止遍在蛋白的转移来实现。 OTUB1还抑制UBE2D和UBE2E家族的E2。在这里我们阐明了OTUB1结合E2s抑制泛素转移的结构机制。 OTUB1通过与供体泛素和E2酶接触来识别带有泛素的E2。出人意料的是，游离泛素与OTUB1上的典型远端泛素结合位点缔合，从而促进了抑制的E2复合物的形成。供体遍在蛋白的Lys48位于OTUB1催化位点和游离遍在蛋白的C末端附近，该构型模拟了与Lys48连接的遍在蛋白链裂解的产物。因此，OTUB1选择Lys48连接的泛素链识别来抑制泛素结合和DNA损伤反应。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号