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首页> 美国卫生研究院文献>other >Interaction Of Histone mRNA Hairpin With Stem-Loop Binding Protein And Regulation Of The SLBP-RNA Complex By Phosphorylation And Proline Isomerization
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Interaction Of Histone mRNA Hairpin With Stem-Loop Binding Protein And Regulation Of The SLBP-RNA Complex By Phosphorylation And Proline Isomerization

机译：用茎环结合蛋白与磷酸盐和脯氨酸异构化与STBP-RNA复合物调节组蛋白mRNA发夹的相互作用

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In metazoans, the majority of histone proteins are generated from replication-dependent histone mRNAs. These mRNAs are unique in that they are not polyadenylated but have a stem-loop structure in their 3′ untranslated region. An early event in 3′ end formation of histone mRNAs is the binding of Stem-Loop Binding Protein (SLBP) to the stem-loop. Here we provide insight into the mechanism by which SLBP contacts the histone mRNA. There are two binding sites in the SLBP RBD for the histone mRNA hairpin. The first binding site (Glu129-Val158) consists of a helix-turn-helix (HTH) motif that likely recognizes the unpaired uridines in the loop of the histone hairpin and upon binding, destabilizes the first G-C base-pair at the base of the stem. The second binding site lies between residues Arg180-Pro200 which appears to recognize the second G-C basepair from the base of the stem and possibly regions flanking the stem-loop. We show that the SLBP-histone mRNA complex is regulated by threonine phosphorylation and proline isomerization in a conserved TPNK sequence that lies between the two binding sites. Threonine phosphorylation increases the affinity of SLBP for histone mRNA by slowing the off-rate for complex dissociation whereas the adjacent proline acts as a critical hinge that may orient the second binding site for formation of a stable SLBP-histone mRNA complex. The NMR and kinetic studies presented here provide a framework for understanding how SLBP recognizes histone mRNA and highlight possible structural roles of phosphorylation and proline isomerization in RNA-binding proteins in remodeling ribonucleoprotein complexes.
机译：在甲唑烷中，大多数组蛋白蛋白质由复制依赖性组蛋白mRNA产生。这些MRNA是独一无二的，因为它们不是聚酰基化但在其3'未翻译区域中具有茎环结构。组蛋白mRNA的3'结束形成的早期事件是茎环结合蛋白（SLBP）与茎环的结合。在这里，我们提供了对SLBP接触组蛋白mRNA的机制的洞察力。 SLBP RBD中有两个结合位点，用于组蛋白mRNA发夹。第一结合位点（GLU129-VAL158）由螺旋转螺旋（HTH）主题组成，其可能识别组蛋白发夹的环中的未配对尿素，并且在结合后，使第一GC基对在底部稳定干。第二结合位点位于残留物arg180-Pro200之间，该似乎似乎从杆的底部识别第二G-C基座，并且可能是螺旋环的可能区域。我们表明SLBP-组蛋白mRNA复合物由苏氨酸磷酸化和脯氨酸异构化以保守的TPNK序列调节，其位于两个结合位点之间。苏氨酸磷酸化通过减缓复杂解离的偏移来增加组蛋白mRNA的SLBP的亲和力，而相邻的脯氨酸用作临界铰链，其可以将第二结合位点定向形成稳定的SLBP-组蛋白mRNA复合物。本文呈现的NMR和动力学研究提供了一种框架，用于理解SLBP如何识别组蛋白mRNA，并突出磷酸化和脯氨酸异构化在RNA结合蛋白中重塑中的核糖核蛋白复合物中的培养基和脯氨酸异构化的结构作用。

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