4 YEAST SPLICEOSOMAL PROTEINS (PRP5, PRP9, PRP11, AND PRP21) INTERACT TO PROMOTE U2 SNRNP BINDING TO PREMESSENGER RNA
4 YEAST SPLICEOSOMAL PROTEINS (PRP5, PRP9, PRP11, AND PRP21) INTERACT TO PROMOTE U2 SNRNP BINDING TO PREMESSENGER RNA
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DOI：
10.1101/gad.7.10.1909
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发表时间：
1993-10-01
影响因子：
10.5
通讯作者：
ABELSON, J
中科院分区：
文献类型：
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作者：
RUBY, SW;CHANG, TH;ABELSON, J
我们分析了几种pre-mRNA加工（PRP）蛋白在酵母剪接体形成中的功能。本研究表明，在体外剪接过程中，U2 snRNP需要PRP5（一种DEAD盒状解旋酶样蛋白）、PRP9和PRP11才能与剪接前体结合。对其功能的遗传分析表明，它们和另一种蛋白PRP21协同作用和/或相互作用，并与U2 snRNA的茎环IIa相互作用，将U2 snRNP结合到pre-mRNA上。生化互补实验也表明PRP9和PRP11蛋白相互作用。PRP9和PRP11蛋白在酵母和哺乳动物细胞中的功能可能相似。对ATP和解旋酶样PRPS蛋白的需求表明，这些因素可能促进U2 snRNP与前mrna结合所需的构象变化（涉及U1或U2 snRNP）。
We have analyzed the functions of several pre-mRNA processing (PRP) proteins in yeast spliceosome formation. Here, we show that PRP5 (a DEAD box helicase-like protein), PRP9, and PRP11 are each required for the U2 snRNP to bind to the pre-spliceosome during spliceosome assembly in vitro. Genetic analyses of their functions suggest that they and another protein, PRP21, act concertedly and/or interact physically with each other and with the stem-loop IIa of U2 snRNA to bind U2 snRNP to the pre-mRNA. Biochemical complementation experiments also indicate that the PRP9 and PRP11 proteins interact. The PRP9 and PRP11 proteins may be functioning similarly in yeast and mammalian cells. The requirement for ATP and the helicase-like PRPS protein suggests that these factors might promote a conformational change (involving either the U1 or U2 snRNP) that is required for the association of U2 snRNP with the pre-mRNA.