Functional association of U2 snRNP with the ATP-independent spliceosomal complex E
Functional association of U2 snRNP with the ATP-independent spliceosomal complex E
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DOI：
10.1016/s1097-2765(00)80318-4
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发表时间：
2000-05-01
期刊：
影响因子：
16
通讯作者：
Reed, R
中科院分区：
文献类型：
--
作者：
Das, R;Zhou, ZL;Reed, R
在目前的剪接体组装模型中，U1 snRNP结合到E复合物中的5'剪接位点，然后U2 snRNP以ATP依赖性结合到A复合物中的分支点序列（BPS）。在这里，我们报告的高度纯化，功能性E复合物的表征。我们提供的证据表明，这个复杂的包含功能U2 snRNP和这个snRNP是E复杂的组装所需的。在E复合物中，U2 snRNP结合不需要BPS。这些数据表明了一个剪接体组装模型，其中U1和U2 snRNP首先与E复合体中的剪接体结合，然后ATP依赖性步骤导致U2 snRNP与A复合体中的BPS高度稳定地结合。
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.