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

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• 作者：Chukwudi Ezeokonkwo ; Mohamed A. Ghazy¹ ; Alexander Zhelkovsky² ; Pei-Chun Yeh ; Claire Moore ; ^{Claire.moore@tufts.edu}
• 关键词：CF I ; cleavage factor I ; CPF ; cleavage/polyadenylation factor ; CPSF ; cleavage/polyadenylation specificity factor ; DTT ; dithiothreitol ; GAD ; gal activation domain ; GBD ; gal binding domain ; GST ; glutathione S-transferase ; PAP ; poly(A) polymerase ; PMSF ; phen
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：24 April, 2012
• 卷：586
• 期：8
• 页码：1173-1178
• 文件大小：766 K

摘要

Addition of poly(A) to the 3鈥?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鈥?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 interactions

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