Nucleic Acids Research, 1992, Vol. 20, No. 19 5017-5025
© 1992
MOLECULAR BIOLOGY |
Interaction of hnRNP A1 with snRNPs and pre-mRNAs: evidence for a possible role of A1 RNA annealing activity in the first steps of spliceosome assembly
Istituto di Genetica Biochimica ed Evoluzionistica, CNR Via Abbiategrasso 207-27100 Pavia, Italy
* To whom correspondence should be addressed
Received July 30, 1992. Revised September 10, 1992. Accepted September 10, 1992.
The in vitro interaction of recombinant hnRNP A1 with purified snRNPs and with pre-mRNAs was investigated. We show that protein A1 can stably bind U2 and U4 snRNP but not U1. Oligo-RNAse H cleavage of U2 nucleotides involved in base pairing with the branch site, totally eliminates the A1-U2 interaction. RNase T1 protection and immunopreclpitation experiments demonstrate that recombinant protein A1 specifically binds the 3'-end regions of both ß-globin and Ad-2 introns. However, while on the ß-globln intron only binding to the polypyrimidine tract was observed, on the Ad-2 intron a 32 nt fragment encompassing the branch point and the AG splice-site dinucleotide was bound and protected. Such protection was drastically reduced In the presence of U2 snRNP. Altogether these results indicate that protein A1 can establish a different pattern of association with different pre-mRNAs and support the hypothesis that this protein could play a role in the annealing of U2 to the branch site and hence in the early events of pre-splicing complex assembly.
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