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首页> 外文OA文献 >Processivity of the Saccharomyces cerevisiae Poly(A) Polymerase Requires Interactions at the Carboxyl-Terminal RNA Binding Domain
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Processivity of the Saccharomyces cerevisiae Poly(A) Polymerase Requires Interactions at the Carboxyl-Terminal RNA Binding Domain

机译：酿酒酵母Poly（A）聚合酶的可加工性需要在羧基末端RNA结合域的相互作用。

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摘要

The interaction of the Fip1 subunit of polyadenylation factor I with the Saccharomyces cerevisiae poly(A) polymerase (PAP) was assayed in vivo by two-hybrid analysis and was found to involve two separate regions on PAP, located at opposite ends of the protein sequence. In vitro, Fip1 blocks access of the RNA primer to an RNA binding site (RBS) that overlaps the Fip1 carboxy-terminal interaction region and, in doing so, shifts PAP to a distributive mode of action. Partial truncation of this RBS has the same effect, indicating that this site is required for processivity. A comparison of the utilization of ribo- and deoxyribonucleotides as substrates indicates the existence on PAP of a second RBS which recognizes the last three nucleotides at the 3′ end of the primer. This site discriminates against deoxyribonucleotides at the 3′ end, and interactions at this site are not affected by Fip1. Further analysis revealed that the specificity of PAP for adenosine is not simply a function of the ATP binding site but also reflects interactions with bases at the 3′ end of the primer and at another contact site 14 nucleotides upstream of the 3′ end. These results suggest that the unique specificity of PAP for ribose and base, and thus the extent and type of activity with different substrates, depends on interactions at multiple nucleotide binding sites.
机译：体内通过两个杂交分析法测定了聚腺苷酸化因子I的Fip1亚基与酿酒酵母聚（A）聚合酶（PAP）的相互作用，发现该过程涉及PAP上两个独立的区域，分别位于蛋白质序列的相对末端。在体外，Fip1阻止RNA引物进入与Fip1羧基末端相互作用区域重叠的RNA结合位点（RBS），并在此过程中将PAP转变为分布作用模式。此RBS的部分截短具有相同的效果，表明该位点是进行合成所必需的。核糖核苷酸和脱氧核糖核苷酸作为底物的利用的比较表明，PAP上存在第二个RBS，该RBS识别引物3'端的最后三个核苷酸。该位点在3'端与脱氧核糖核苷酸区分开，并且该位点的相互作用不受Fip1的影响。进一步的分析表明，PAP对腺苷的特异性不仅是ATP结合位点的功能，而且还反映了与引物3'端的碱基以及3'端上游14个核苷酸的另一个接触位点的碱基相互作用。这些结果表明PAP对核糖和碱基的独特特异性，以及因此与不同底物的活性的程度和类型，取决于多个核苷酸结合位点的相互作用。

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