Functional association of U2 snRNP with the ATP-independent spliceosomal complex E.
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Das R, Zhou Z, Reed R
Functional association of U2 snRNP with the ATP-independent spliceosomal complex E.
Mol Cell. 2000 May;5(5):779-87.
- PubMed ID
- 10882114 [ View in PubMed]
- Abstract
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.