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首页> 外文期刊>Molecular and Cellular Biology >Multiple interactions between the splicing substrate and small nuclear ribonucleoproteins in spliceosomes.
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Multiple interactions between the splicing substrate and small nuclear ribonucleoproteins in spliceosomes.

机译：剪接底物和剪接体中的小核糖核糖核蛋白之间的多重相互作用。

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摘要

Protection experiments with antibodies against small nuclear ribonucleoproteins (snRNPs) have elucidated the location of and requirements for interactions between snRNPs and human beta-globin transcripts during splicing in vitro. U2 snRNP association with the intron branch site continues after branch formation, requires intact U2 RNA, and is affected by some alterations of the 3' splice site sequence. U2 snRNP binding to the branched intermediate and U1 snRNP protection of an extended 5' splice region are detected exclusively in spliceosome fractions, indicating that both snRNPs are spliceosome components. While each snRNP associates specifically with the pre-mRNA, they also appear to interact with each other. The recovery of fragments mapping upstream of the 5' splice site suggests how the excised exon is held in the spliceosome.
机译：用抗小核糖核糖核蛋白（snRNPs）的抗体进行的保护实验已经阐明了在体外剪接过程中snRNPs与人β-珠蛋白转录本之间相互作用的位置和要求。 U2 snRNP与内含子分支位点的结合在分支形成后继续，需要完整的U2 RNA，并受3'剪接位点序列的某些改变的影响。仅在剪接体级分中检测到了U2 snRNP与分支中间物的结合以及U1 snRNP对扩展的5'剪接区的保护，这表明两个snRNP均为剪接体组件。尽管每个snRNP都与前mRNA特异性结合，但它们似乎也相互作用。定位在5'剪接位点上游的片段的回收表明，切除的外显子如何保持在剪接体中。

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