Patterns and plasticity in RNA-protein interactions enable recruitment of multiple proteins through a single site
Patterns and plasticity in RNA-protein interactions enable recruitment of multiple proteins through a single site
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DOI：
10.1073/pnas.1200521109
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发表时间：
2012-04-17
影响因子：
11.1
通讯作者：
Wickens, Marvin
中科院分区：
文献类型：
--
作者：
Valley, Cary T.;Porter, Douglas F.;Wickens, Marvin
信使核糖核酸的调控取决于蛋白质对其RNA结合部位的特异性和亲和力。调控蛋白必须结合它们自己的位点，甚至拒绝密切相关的非同源位点。在PUF[Pumilio和Fem-3结合因子(FBF)]RNA结合蛋白家族中，单个蛋白质区分结合位点的长度和序列的差异，使每个PUF能够结合不同的mRNAs。在这里，我们表明，尽管有这些差异，RNA相互作用的模式在PUF蛋白之间是保守的：PUF蛋白的两端与RNA位点的两端进行关键接触。尽管这种保守的“双手”识别模式，但RNA序列是灵活的。在酵母Puf4p的结合位点中，RNA序列决定了RNA碱基从蛋白质结合表面翻转的模式。RNA序列上的微小差异允许新的控制模式，在单个位点招募Puf5p和Puf4p。这种嵌入的信息为RNA靶标和PUF蛋白之间的连接增加了一层新的生物学意义。
mRNA control hinges on the specificity and affinity of proteins for their RNA binding sites. Regulatory proteins must bind their own sites and reject even closely related noncognate sites. In the PUF [Pumilio and fem-3 binding factor (FBF)] family of RNA binding proteins, individual proteins discriminate differences in the length and sequence of binding sites, allowing each PUF to bind a distinct battery of mRNAs. Here, we show that despite these differences, the pattern of RNA interactions is conserved among PUF proteins: the two ends of the PUF protein make critical contacts with the two ends of the RNA sites. Despite this conserved "two-handed" pattern of recognition, the RNA sequence is flexible. Among the binding sites of yeast Puf4p, RNA sequence dictates the pattern in which RNA bases are flipped away from the binding surface of the protein. Small differences in RNA sequence allow new modes of control, recruiting Puf5p in addition to Puf4p to a single site. This embedded information adds a new layer of biological meaning to the connections between RNA targets and PUF proteins.