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首页> 外文期刊>Journal of Molecular Biology >Dephosphorylation of RNA Polymerase II by CTD-phosphatase FCP1 is Inhibited by Phospho-CTD Associating Proteins.
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Dephosphorylation of RNA Polymerase II by CTD-phosphatase FCP1 is Inhibited by Phospho-CTD Associating Proteins.

机译：磷酸CTD相关蛋白抑制CTD磷酸酶FCP1对RNA聚合酶II的去磷酸化。

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摘要

Reversible phosphorylation of the repetitive C-terminal domain (CTD) of the largest RNA polymerase (RNAP) II subunit plays a key role in the progression of RNAP through the transcription cycle. The level of CTD phosphorylation is determined by multiple CTD kinases and a CTD phosphatase, FCP1. The phosphorylated CTD binds to a variety of proteins including the cis/trans peptidyl-prolyl isomerase (PPIase) Pin1 and enzymes involved in processing of the primary transcript such as the capping enzyme Hce1 and CA150, a nuclear factor implicated in transcription elongation. Results presented here establish that the dephosphorylation of hyperphosphorylated RNAP II (RNAP IIO) by FCP1 is impaired in the presence of Pin1 or Hce1, whereas CA150 has no influence on FCP1 activity. The inhibition of dephosphorylation is observed with free RNAP IIO generated by different CTD kinases as well as with RNAP IIO engaged in an elongation complex. These findings support the idea that specific phospho-CTD associating proteins can differentially modulate the dephosphorylation of RNAP IIO by steric hindrance and may play an important role in the regulation of gene expression.
机译：最大的RNA聚合酶（RNAP）II亚基的重复性C末端结构域（CTD）的可逆磷酸化在RNAP通过转录循环的进程中起着关键作用。 CTD磷酸化的水平由多种CTD激酶和CTD磷酸酶FCP1决定。磷酸化的CTD与多种蛋白质结合，包括顺式/反式肽基-脯氨酰脯氨酰异构酶（PPIase）Pin1和涉及初级转录本加工的酶，例如加帽酶Hce1和CA150，这是与转录延伸有关的核因子。此处显示的结果表明，在存在Pin1或Hce1的情况下，FCP1对高磷酸化RNAP II（RNAP IIO）的去磷酸化作用会受到损害，而CA150对FCP1活性没有影响。观察到由不同的CTD激酶产生的游离RNAP IIO以及参与延伸复合物的RNAP IIO对去磷酸化的抑制。这些发现支持这样的想法，即特定的磷酸-CTD缔合蛋白可以通过位阻差异地调节RNAP IIO的去磷酸化，并且可能在基因表达的调节中起重要作用。

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