乌比基因通过一种新的pleckstrin-homology域相互作用对蛋白质组进行对接
Patrick Schreiner1, Xiang Chen, Koraljka Husnjak
1Center for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany.
Nature
|May 24, 2008
概括
Rpn13作为蛋白酶体的新型泛素受体,利用独特的循环结构来结合泛素. 这一发现澄清了蛋白质体基质的识别,并将乌比基结合与Uch37.7.的二维基基化联系起来.
科学领域:
- 分子生物学分子生物学
- 结构生物学 结构生物学
- 生物化学 生物化学
背景情况:
- 向性蛋白质降解依赖于无素-蛋白酶体通路.
- 蛋白质体基质识别机制尚未完全理解.
- Rpn10/S5a是已确立的蛋白质体泛素受体,但在酵母中并不重要.
研究的目的:
- 为了阐明Rpn13.的泛素结合机制.
- 描述Rpn13作为蛋白质体内泛素受体的作用.
- 为了了解Rpn13对子基质如何从ubiquitination转化为deubiquitination.
主要方法:
- 晶体学和NMR光谱学以确定Rpn13结构.
- 生物化学测试以评估Rpn13的结合能力.
- 结构建模 Rpn13 复合与二维基素.
主要成果:
- 确定了单独Rpn13的结构和与ubiquitin复合的结构.
- Rpn13采用了一种基于循环的全新机制来结合乌比奎丁.
- Rpn13同时与ubiquitin和蛋白酶子单元Rpn2/S1.1.结合在一起.
- 通过duibiquitin生成了Rpn13的模型结构.
结论:
- Rpn13作为蛋白质酶体的关键无素受体起作用.
- Rpn13使用一种独特的结构机制来捕获ubiquitin.
- Rpn13的双重结合能力支持其在基质降解和二氧化调节中的作用.
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