Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae.

FEBS Letters
Chukwudi EzeokonkwoClaire L Moore

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.

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Citations

Oct 23, 2012·Biochimica Et Biophysica Acta·Hannah E Mischo, Nick J Proudfoot
Mar 5, 2014·Molecular and Cellular Biology·Kehui XiangJames L Manley
Jan 27, 2019·The Journal of Biological Chemistry·Murray Stewart
Nov 28, 2020·Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms·Nadra Al-HusiniAthar Ansari

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