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首页> 外文期刊>The Journal of biological chemistry >Solution Structure of Tandem SH2 Domains from Spt6 Protein and Their Binding to the Phosphorylated RNA Polymerase II C-terminal Domain
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Solution Structure of Tandem SH2 Domains from Spt6 Protein and Their Binding to the Phosphorylated RNA Polymerase II C-terminal Domain

机译：SPT6蛋白的串联SH2结构域的溶液结构及其与磷酸化RNA聚合酶II C-末端结构域的结合

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摘要

Spt6 is a highly conserved transcription elongation factor and histone chaperone. It binds directly to the RNA polymerase II C-terminal domain (RNAPII CTD) through its C-terminal region that recognizes RNAPII CTD phosphorylation. In this study, we determined the solution structure of the C-terminal region of Saccharomyces cerevisiae Spt6, and we discovered that Spt6 has two SH2 domains in tandem. Structural and phylogenetic analysis revealed that the second SH2 domain was evolutionarily distant from canonical SH2 domains and represented a novel SH2 subfamily with a novel binding site for phosphoserine. In addition, NMR chemical shift perturbation experiments demonstrated that the tandem SH2 domains recognized Tyr1, Ser2, Ser5, and Ser7 phosphorylation of RNAPII CTD with millimolar binding affinities. The structural basis for the binding of the tandem SH2 domains to different forms of phosphorylated RNAPII CTD and its physiological relevance are discussed. Our results also suggest that Spt6 may use the tandem SH2 domain module to sense the phosphorylation level of RNAPII CTD.
机译：SPT6是一种高度保守的转录伸长因子和组蛋白伴侣。它通过其识别RNAPII CTD磷酸化的C末端区域直接与RNA聚合酶II C-末端结构域（RNAPII CTD）结合。在这项研究中，我们确定了酿酒酵母SPT6的C末端区域的溶液结构，我们发现SPT6在串联中具有两个SH2结构域。结构和系统发育分析表明，第二SH2结构域与规范SH2结构域进化地，并用新的磷素结合位点代表新的SH2亚家族。此外，NMR化学型扰动实验表明，串联SH2结构域通过毫米摩尔结合亲和力公认抗ry1，ser2，ser5和rnapii ctd的Ser7磷酸化。讨论了串联SH2结构域与不同形式的磷酸化RNAPII CTD的结构基础及其生理相关性。我们的结果还表明SPT6可以使用串联SH2域模块来感测RNAPII CTD的磷酸化水平。

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