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聚腺苷酸化酶基本 N 端的新相互作用,可调节酿酒酵母中的聚腺苷酸化添加。

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

机构信息

Tufts School of Medicine and the Sackler Graduate School of Biomedical Sciences, Boston, MA 02111, USA.

出版信息

FEBS Lett. 2012 Apr 24;586(8):1173-8. doi: 10.1016/j.febslet.2012.03.036. Epub 2012 Mar 24.

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.

摘要

在酵母中,断裂前 mRNA 的 3' 端添加 poly(A) 对于 mRNA 成熟是必不可少的,该过程由 Pap1 催化。我们之前已经表明,缺乏前 18 个氨基酸的非活性 Pap1 突变体完全能够对寡聚 A 进行多聚腺苷酸化,但对于前 mRNA 多聚腺苷酸化却是有缺陷的,这表明 N 端的相互作用对于酶在加工复合物中的功能很重要。我们现在已经鉴定出与该区域特异性相互作用的蛋白质。Cft1 和 Pta1 是切割/多聚腺苷酸化因子的亚基,Pap1 就位于其中,而 Nab6 和 Sub1 是具有已知与 3' 端加工相关的核酸结合蛋白。我们的结果表明了一种控制 Pap1 活性的新机制,并讨论了可能涉及这些新发现的相互作用的模型。

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