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Mol. Cell. Biol., Oct 1995, 5750-5756, Vol 15, No. 10
Copyright © 1995, American Society for Microbiology

Accumulation of a novel spliceosomal complex on pre-mRNAs containing branch site mutations

P Champion-Arnaud, O Gozani, L Palandjian and R Reed
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

Pre-mRNA assembles into spliceosomal complexes in the stepwise pathway E-->A-->B-->C. We show that mutations in the metazoan branchpoint sequence (BPS) have no apparent effect on E complex formation but block the assembly of the A complex and the UV cross-linking of U2 small nuclear ribonucleoprotein particle (snRNP) proteins. Unexpectedly, a novel complex, designated E*, assembles on pre-mRNAs containing BPS mutations. Unlike the E complex, the E* complex accumulates in the presence of ATP. U1 snRNP and U2AF, which are tightly bound to pre-mRNA in the E complex, are not tightly bound in the E* complex. Significantly, previous work showed that U1 snRNP and U2AF become destabilized from pre-mRNA after E complex assembly on normal pre- mRNAs. Thus, our data are consistent with a model in which there are two steps in the transition from the E complex to the A complex (E-->E*- ->A). In the first step, U1 snRNP and U2AF are destabilized in an ATP- dependent, BPS-independent reaction. In the second step, the stable binding of U2 snRNP occurs in a BPS-dependent reaction.


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