在结合体激活过程中B复合蛋白招募的动力学和进化保存
Xingyang Fu1, Aaron A Hoskins1,2
1Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, United States.
Nucleic acids research
|February 25, 2025
概括
包括Prp38,Snu23和Spp381在内的B组合蛋白 (BCP) 亚组合,同时结合结合体,并在酵母和人类中保存. ATP水平影响BCP蛋白招募,可能调节拼接.
科学领域:
- 分子生物学分子生物学
- 在RNA生物学,RNA生物学.
- 生物化学 生物化学
背景情况:
- 结合酶组件的组装涉及动态的蛋白质和RNA相互作用.
- 在激活过程中,B复合体特定蛋白 (Prp38,Snu23,Spp381) 稳定了结合体.
- 对于BCP蛋白招募到spliceosomes的机制尚未完全理解.
研究的目的:
- 为了可视化Prp38,Snu23和Spp381在spliceosome组装过程中的实时动态.
- 研究BCP蛋白的招募和释放机制.
- 为了确定ATP度在BCP蛋白协会中的作用.
主要方法:
- 定位单分子光谱学 (CoSMoS) 用于研究蛋白质动力学.
- 实时观察spliceosome组装在体外.
- 在不同的ATP条件下分析BCP蛋白与前mRNA和结合酶体的关联.
主要成果:
- BCP 蛋白质 (Prp38,Snu23,Spp381) 同时从结合酶体中结合和释放,表明一个稳定的亚复合体.
- 在U4 snRNP解离和NTC结合后,BCP蛋白与三snRNP结合和释放后与前mRNA结合.
- 低ATP度导致BCP与tri-snRNP的前关联,使其能够同时与前mRNA结合.
结论:
- 在Saccharomyces cerevisiae和人类之间,BCP蛋白对结合体的招募是保留的.
- BCP 蛋白质在结合体内形成一个潜在的子复合体.
- 在低ATP下,与tri-snRNP结合的BCP蛋白可能通过形成非生产性复合体来调节拼接.
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