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Vol. 14, No. 4, pp. 403-413, February 15, 2000
European Molecular Biology Laboratory
(EMBL), 69117 Heidelberg, Germany
Although it has been established that the processing factors
involved in pre-mRNA splicing and 3'-end formation can influence each other positively, the molecular basis of this coupling interaction was not known. Stimulation of pre-mRNA splicing by an adjacent cis-linked cleavage and polyadenylation site in HeLa cell
nuclear extract is shown to occur at an early step in splicing, the
binding of U2AF 65 to the pyrimidine tract of the intron 3' splice
site. The carboxyl terminus of poly(A) polymerase (PAP) previously has been implicated indirectly in the coupling process. We demonstrate that
a fusion protein containing the 20 carboxy-terminal amino acids of PAP,
when tethered downstream of an intron, increases splicing efficiency
and, like the entire 3'-end formation machinery, stimulates U2AF 65 binding to the intron. The carboxy-terminal domain of PAP makes a
direct and specific interaction with residues 17-47 of U2AF 65, implicating this interaction in the coupling of splicing and 3'-end formation.
[Key Words: RNA processing; cleavage; polyadenylation; splicing; poly(A) polymerase; U2AF 65]
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