人类simpllekin-Ssu72-CTD合体复合物的晶体结构
Kehui Xiang1, Takashi Nagaike, Song Xiang
1Department of Biological Sciences, Columbia University, New York, New York 10027, USA.
Nature
|September 24, 2010
概括
这些都是症状.
科学领域:
- 分子和结构生物学 分子和结构生物学
- RNA 处理和基因调控
背景情况:
- 辛普莱肯是真核细胞信使RNA (mRNA前) 处理中的关键支架蛋白.
- 它在 RNA 聚合酶 II (Pol II) 的多基化和转录中的精确分子功能仍然不清楚.
研究的目的:
- 阐明simplekin在mRNA前3'-end处理中的作用的结构基础.
- 为了研究simplekin,Ssu72酸酶和Pol IICTD之间的相互作用.
主要方法:
- 在三元复合体中,人类simpllekin的N终端域的X射线晶体学.
- 生物化学试验以评估Ssu72酸酶活性和多基化在体外.
主要成果:
- 用Ssu72和CTD光的方法确定了simplekin的N端域的2.4 Å晶体结构.
- 揭示了simplekin的ARM/HEAT折叠以及它与Ssu72.2的交互界面.
- 证明simplekin刺激Ssu72活动并抑制转录合的多基解.
结论:
- 辛普莱克的N端域直接与Ssu72相互作用,调节其酸酶活性.
- 哺乳动物Ssu72在转录合的mRNA前3'-end处理中起着至关重要的作用,受 symplekin的影响.
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