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首页> 外文期刊>Protein and peptide letters >The Interaction Between Two Arabidopsis Polyadenylation Factor Subunits Involves an Evolutionarily-Conserved Motif and Has Implications for the Assembly and Function of the Polyadenylation Complex
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The Interaction Between Two Arabidopsis Polyadenylation Factor Subunits Involves an Evolutionarily-Conserved Motif and Has Implications for the Assembly and Function of the Polyadenylation Complex

机译：两个拟南芥属聚腺苷酸化因子亚基之间的相互作用涉及进化保守的主题，对聚腺苷酸化复合物的组装和功能具有影响

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The polyadenylation factor subunit “Factor Interacting with Poly(A) polymerase” (Fip1) is an important bridging subunit in the eukaryotic polyadenylation complex. To better understand the functioning of Fip1 in Arabidopsis, a random combinatorial screen for peptides that interact with a conserved plant-specific domain in the protein was conducted. A search of the Arabidopsis proteome using these Fip1-binding peptides as queries resulted in the identification of a number of putative Fip1-interacting proteins. One of these was the polyadenylation factor subunit, CstF77. This purported interaction was confirmed by yeast two-hybrid and in vitro assays. Mutation of the motif identified in the phage display screen eliminated the interaction, corroborating the results of the phage display screen. The domain of CstF77 that interacts with Fip1 lies at its extreme C-terminus and is distinct from the part of CstF77 that binds CstF64. Taken together, these results suggest that Fip1 is situated near CstF64 in the polyadenylation complex.
机译：聚腺苷酸化因子亚基“与聚（A）聚合酶相互作用的因子”（Fip1）是真核生物聚腺苷酸化复合物中一个重要的桥接亚基。为了更好地了解Fip1在拟南芥中的功能，对与蛋白质中保守的植物特异性结构域相互作用的肽进行了随机组合筛选。使用这些与Fip1结合的肽作为查询对象的拟南芥蛋白质组的搜索导致鉴定了许多推定的与Fip1相互作用的蛋白。其中之一是聚腺苷酸化因子亚基CstF77。这种声称的相互作用已通过酵母双杂交和体外试验得到证实。在噬菌体显示屏中鉴定出的基序突变消除了相互作用，从而证实了噬菌体显示屏的结果。与Fip1相互作用的CstF77域位于其最末端的C末端，与CstF77绑定CstF64的部分不同。综上所述，这些结果表明，Fip1位于聚腺苷酸复合物中的CstF64附近。

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