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首页> 外文期刊>Biochemistry >Phosphorylation of RNA polymerase IICTD fragments results in tight bindingto the WW domain from the yeast prolyl isomerase Ess1
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Phosphorylation of RNA polymerase IICTD fragments results in tight bindingto the WW domain from the yeast prolyl isomerase Ess1

机译：RNA聚合酶IICTD片段的磷酸化导致与酵母脯氨酰异构酶Ess1的WW域紧密结合

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摘要

The yeast prolyl isomerase, Ess1, has recently been shown to interact via its WW domain with the hyperphosphorylated form of the RNA polymerase II C-terminal domain (CTD). We have investigated folding of the Ess1 WW domain and its binding to peptides representing the CTD by circular dichroism and fluorescence. Ess1 WW folds and unfolds reversibly, but in the absence of ligand is only marginally stable with a melting temperature of 19 degreesC. The WW domain is stabilized by the addition of anionic ligands, namely, chloride, inorganic phosphate, phosphoserine, and phosphorylated CTD peptides. Dissociation constants were measured to be 70-100 muM for CTD peptides phosphorylated at one serine, and 16-21 muM for peptides with two or more phosphorylated serines. Weaker or no affinity was observed for nonphosphorylated CTD peptides. There is surprisingly little difference in the affinity for peptides phosphorylated at Ser 2 or Ser 5 of the consensus repeat, or for peptides with different patterns of multiple phosphorylation. The binding of Ess1 to phosphorylated CTD peptides is consistent with a model wherein the WW domain positions Ess1 to catalyze isomerization of the many pSer-Pro peptide bonds in the phosphorylated CTD. We suggest that cis/trans isomerization of prolyl peptide bonds plays a crucial role in CTD function during eukaryotic transcription.
机译：酵母脯氨酰异构酶，Ess1，最近已显示通过其WW域与RNA聚合酶II C末端域（CTD）的超磷酸化形式相互作用。我们已经研究了Ess1 WW结构域的折叠及其通过圆二色性和荧光与代表CTD的肽的结合。 Ess1 WW可逆地折叠和展开，但在没有配体的情况下，其熔融温度为19摄氏度时仅略微稳定。 WW域通过添加阴离子配体（即氯化物，无机磷酸盐，磷酸丝氨酸和磷酸化CTD肽）来稳定。对于在一个丝氨酸上磷酸化的CTD肽，测得的解离常数为70-100μM，对于具有两个或多个磷酸化丝氨酸的肽，测得的解离常数为16-21μM。对于非磷酸化的CTD肽没有观察到较弱或没有亲和力。对于在共有重复序列的Ser 2或Ser 5处磷酸化的肽，或在具有多种磷酸化模式的肽上，亲和力几乎没有差异。 Ess1与磷酸化CTD肽的结合与模型相符，其中WW结构域将Ess1定位为催化磷酸化CTD中许多pSer-Pro肽键的异构化。我们建议在真核转录过程中脯氨酰肽键的顺/反异构化在CTD功能中起着至关重要的作用。

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