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    Mol Cell. 2000 May;5(5):779-87.

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

    Das R, Zhou Z, Reed R.

    Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

    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.

    PMID: 10882114 [PubMed - indexed for MEDLINE]

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