在分裂细胞激活过程中B复合蛋白招募的动力学和进化保护
Xingyang Fu1,2, Aaron A Hoskins1,3
1Department of Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.
bioRxiv : the preprint server for biology
|August 16, 2024
概括
由Prp38,Snu23和Spp381组成的B复合蛋白 (BCP) 亚复合体同时结合结合体. 这种保存的招募途径对结合体激活至关重要,并可能调节结合.
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:
- 剪切酶组装是一个动态的过程,涉及许多蛋白质和snRNA相互作用.
- 在激活过程中,B复合体特异性蛋白 Prp38,Snu23 和 Spp381 对于稳定结合酶体至关重要.
- 了解这些蛋白质的招募机制是破译结合体动态的关键.
研究的目的:
- 为了可视化Prp38,Snu23和Spp381在spliceosome组装和激活期间的实时动态.
- 描述这些蛋白质的结合和释放模式,与结合体细胞的进展有关.
- 调查ATP度对BCP亚复合体招募的作用.
主要方法:
- 定位单分子光谱学 (CoSMoS) 用于实时监测蛋白质动态.
- 同时观察Prp38,Snu23和Spp381的结合和解结合事件.
- 在整个拼接周期中分析蛋白质与前mRNA和snRNP的关联.
主要成果:
- Prp38,Snu23和Spp381同时从结合体中结合和释放,形成一个稳定的B组合蛋白 (BCP) 亚组合体.
- 在tri-snRNP结合后,BCP与前mRNA结合,并在U4 snRNP解离和NineTeen Complex (NTC) 结合后主要释放.
- 在低ATP条件下,BCP与tri-snRNP进行预结合,从而同时与pre-mRNA结合.
结论:
- 在酵母和人类之间,BCP亚复合体到结合体的招募途径是保留的.
- 在低ATP下,BCP与tri-snRNP的相互作用表明通过形成潜在的非生产性复合体来调节拼接的机制.
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