Abstract
Addition of poly(A) to the 3′ ends of cleaved pre-mRNA is essential for mRNA maturation and is catalyzed by Pap1 in yeast. We have previously shown that a non-viable Pap1 mutant lacking the first 18 amino acids is fully active for polyadenylation of oligoA, but defective for pre-mRNA polyadenylation, suggesting that interactions at the N-terminus are important for enzyme function in the processing complex. We have now identified proteins that interact specifically with this region. Cft1 and Pta1 are subunits of the cleavage/polyadenylation factor, in which Pap1 resides, and Nab6 and Sub1 are nucleic-acid binding proteins with known links to 3′ end processing. Our results suggest a novel mechanism for controlling Pap1 activity, and possible models invoking these newly-discovered interactions are discussed. Structured summary of protein interactionsPAP1binds to Fip1 by anti bait coimmunoprecipitation (View interaction)PAP1binds to Fip1 by pull down (View interaction)PAP1physically interacts with PTA1 by two hybrid (View interaction)PAP1binds to Sub1 by pull down (View interaction)PAP1physically interacts with Fip1 by two hybrid (View Interaction: 1, 2)PAP1binds to Nab6 by pull down (View interaction)Nab6physically interacts with PAP1 by two hybrid (View interaction)Cft1binds to PAP1 by pull down (View interaction)PTA1binds to PAP1 by pull down (View interaction)
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