Interaction of U2AF(65) RS region with pre-mRNA of branch point and promotion base pairing with U2 snRNA
Interaction of U2AF(65) RS region with pre-mRNA of branch point and promotion base pairing with U2 snRNA
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DOI：
10.1126/science.273.5282.1706
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发表时间：
1996-09-20
期刊：
影响因子：
56.9
通讯作者：
Green, MR
中科院分区：
文献类型：
--
作者：
Valcarcel, J;Gaur, RK;Green, MR
哺乳动物剪接因子U2 AF（65）与3'剪接位点附近的多聚嘧啶段结合，并促进U2小核核糖核蛋白在上游分支点的组装，这种相互作用涉及与U2小核RNA（snRNA）的碱基配对。U2 AF（65）含有一个RNA结合域，需要与多聚嘧啶段相互作用，和一个富含丝氨酸-丝氨酸（RS）的区域，需要U2 snRNP募集和剪接。本文报道，U2 AF（65）与多聚嘧啶段的结合指导RS域接触分支点，并促进U2 snRNA-分支点碱基配对，即使在没有其他剪接因子的情况下。RS结构域突变体的分析表明，U2 AF（65）接触分支点、促进U2 snRNA-分支点相互作用和支持剪接的能力是相关的活性，仅需要几个碱性氨基酸。因此，U2 AF（65）RS结构域在调节剪接体RNA-RNA相互作用中起直接作用。
The mammalian splicing factor U2AF(65) binds to the polypyrimidine tract adjacent to the 3' splice site and promotes assembly of U2 small nuclear ribonucleoprotein on the upstream branch point, an interaction that involves base pairing with U2 small nuclear RNA(snRNA). U2AF(65) contains an RNA binding domain, required for interaction with the polypyrimidine tract, and an arginine-serine-rich (RS) region, required for U2 snRNP recruitment and splicing, Here it is reported that binding of U2AF(65) to the polypyrimidine tract directed the RS domain to contact the branch point and promoted U2 snRNA-branch point base pairing even in the absence of other splicing factors. Analysis of RS domain mutants indicated that the ability ol U2AF(65) to contact the branch point, to promote the U2 snRNA-branch point interaction, and to support splicing are related activities, requiring only a few basic amino acids. Thus, the U2AF(65) RS domain plays a direct role in modulating spliceosomal RNA-RNA interactions.