snRNP公司
剪接体
生物
RNA剪接
细胞生物学
遗传学
计算生物学
核糖核酸
基因
作者
Rita Das,Zhaolan Zhou,Robin Reed
出处
期刊:Molecular Cell
[Elsevier]
日期:2000-05-01
卷期号:5 (5): 779-787
被引量:166
标识
DOI:10.1016/s1097-2765(00)80318-4
摘要
In the current model for spliceosome assembly, U1 snRNP binds to the 5' splice site in the E complex followed by ATP-dependent binding of U2 snRNP to the branchpoint sequence (BPS) in the A complex. Here we report the characterization of highly purified, functional E complex. We provide evidence that this complex contains functional U2 snRNP and that this snRNP is required for E complex assembly. The BPS is not required for U2 snRNP binding in the E complex. These data suggest a model for spliceosome assembly in which U1 and U2 snRNPs first associate with the spliceosome in the E complex and then an ATP-dependent step results in highly stable U2 snRNP binding to the BPS in the A complex.
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