以E2为媒介的SUMO结合的结构基础是由ubiquitin-conjugating酶Ubc9和RanGAP1之间的复合体揭示的
Victor Bernier-Villamor1, Deborah A Sampson, Michael J Matunis
1Biochemistry Department, Structural Biology Program, Weill Medical College of Cornell University, New York, NY 10021, USA.
Cell
|February 21, 2002
概括
SUMO E2 酶 Ubc9 直接识别和修改 SUMO 标,与大多数无处不在的酶不同. 结构和生化研究揭示了Ubc9的关键动机.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- E2酶将乌比奎和类似乌比奎的蛋白质结合到基质上.
- 小型泛胺类修饰剂 (SUMO) 途径调节关键的细胞过程.
- Ubc9是一种SUMO E2酶,其独特之处在于它能够独立地识别SUMO基质.
研究的目的:
- 为了阐明Ubc9-介导的SUMO结合的结构基础.
- 确定Ubc9基质识别和修改的分子决定因素.
- 研究特定的Ubc9和基底基因在SUMOylation中的作用.
主要方法:
- Ubc9-RanGAP1复合物的X射线晶体学.
- 基于 Ubc9 和 RanGAP1.1 的结构性突变发生.
- 生物化学试验以评估各种基质的SUMOylation.
主要成果:
- 哺乳动物Ubc9与RanGAP1结合的晶体结构揭示了关键的相互作用.
- 在Ubc9和SUMO基板中的独特图案对于识别和修改至关重要.
- 突变性研究证实了这些基因对p53,IkappaBalpha和RanGAP1.1的SUMOylation的重要性.
结论:
- Ubc9 直接在基板内结合 SUMO 共识序列.
- Ubc9中的特定结构动机及其目标决定了SUMOylation的特异性.
- 这项工作提供了对 Ubc9.9 的 SUMO 结合机制的见解.
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