来自Saccharomyces cerevisiae的一个Intron Lariat Spliceosome的结构
Ruixue Wan1, Chuangye Yan1, Rui Bai1
1Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China.
Cell
|September 19, 2017
概括
这项研究揭示了内部拉里亚特结合体 (ILS) 复合体的冷电子显微镜结构. 它详细介绍了特定的拼接因子的释放和Prp43的结合,并提出了ILS拆解的机制.
科学领域:
- 分子生物学
- 结构生物学
- 生物化学
背景情况:
- 在mRNA前拼接过程中,内核拉里亚特拼接体 (ILS) 复合体至关重要.
- 了解ILS的拆卸是理解拼接周期的最后阶段的关键.
研究的目的:
- 确定Saccharomyces cerevisiae ILS复合物的高分辨率冷电子显微镜结构.
- 阐明控制ILS分解的分子机制.
主要方法:
- 使用冷电子显微镜 (cryo-EM) 来获得ILS复合物的结构.
- 结构分析的重点是释放的因素与剩余组件之间的相互作用.
主要成果:
- 结构显示内离子仍然结合,而结合的外离子被解离.
- 主要的拼接因子如Prp17,Prp18,Cwc21和Cwc22从活性部位释放出来.
- Prp43在结合体外围,U6 snRNA附近结合Syf1.
- Ntr1/Spp382和Ntr2分别与Snu114和Prp8相互作用,为该综合体的结构做出了贡献.
结论:
- 确定结构为ILS拆卸过程提供了洞察力.
- 特定的蛋白-RNA和蛋白-蛋白相互作用表明了拼接的最后步骤的机制.
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