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首页> 外文期刊>Molecular and Cellular Biology >Characterization of a U2AF-Independent Commitment Complex (E′) in the Mammalian Spliceosome Assembly Pathway
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Characterization of a U2AF-Independent Commitment Complex (E′) in the Mammalian Spliceosome Assembly Pathway

机译：哺乳动物剪接体组装途径中U2AF独立的承诺复合体（E'）的表征。

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摘要

Early recognition of pre-mRNA during spliceosome assembly in mammals proceeds through the association of U1 small nuclear ribonucleoprotein particle (snRNP) with the 5′ splice site as well as the interactions of the branch binding protein SF1 with the branch region and the U2 snRNP auxiliary factor U2AF with the polypyrimidine tract and 3′ splice site. These factors, along with members of the SR protein family, direct the ATP-independent formation of the early (E) complex that commits the pre-mRNA to splicing. We report here the observation in U2AF-depleted HeLa nuclear extract of a distinct, ATP-independent complex designated E′ which can be chased into E complex and itself commits a pre-mRNA to the splicing pathway. The E′ complex is characterized by a U1 snRNA-5′ splice site base pairing, which follows the actual commitment step, an interaction of SF1 with the branch region, and a close association of the 5′ splice site with the branch region. These results demonstrate that both commitment to splicing and the early proximity of conserved sequences within pre-mRNA substrates can occur in a minimal complex lacking U2AF, which may function as a precursor to E complex in spliceosome assembly.
机译：哺乳动物剪接体组装过程中对pre-mRNA的早期识别是通过U1小核糖核蛋白颗粒（snRNP）与5'剪接位点的结合以及分支结合蛋白SF1与分支区域和U2 snRNP辅助分子的相互作用来进行的具有聚嘧啶束和3'剪接位点的U2AF因子。这些因素，连同SR蛋白家族的成员，指导早期（E）复合体的ATP非依赖性形成，该复合体将前mRNA进行剪接。我们在此报告了在U2AF耗尽的HeLa核提取物中观察到的独特的，非ATP独立的复合物E'的现象，该复合物可被追逐到E复合物中，并且其自身将pre-mRNA提交至剪接途径。 E'复合物的特征在于U1 snRNA-5'剪接位点碱基配对，该配对遵循实际的承诺步骤，SF1与分支区域的相互作用以及5'剪接位点与分支区域的紧密关联。这些结果表明，对剪接的承诺和保守序列在pre-mRNA底物中的早期接近都可以在缺乏U2AF的最小复合物中发生，该复合物可以作为剪接体组装中E复合物的前体。

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