Functional association of U2 snRNP with the ATP-independent spliceosomal complex E

被引：142
作者：
Das, R [1 ]
Zhou, ZL [1 ]
Reed, R [1 ]
机构：
[1] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
来源：
MOLECULAR CELL | 2000年 / 5卷 / 05期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1016/S1097-2765(00)80318-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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.
引用
收藏
页码：779 / 787
页数：9
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