RNA聚合酶II C末端结构域磷酸酶HSPC129的表达与特性分析
Expression and characterization of HSPC129, a RNA polymerase II C-terminal domain phosphatase.
作者信息
Qian Hui, Ji Chaoneng, Zhao Shuo, Chen Jinzhong, Jiang Mei, Zhang Yong, Yan Mi, Zheng Dan, Sun Yaqiong, Xie Yi, Mao Yumin
机构信息
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Room 602, Science Building, Shanghai, PR China.
出版信息
Mol Cell Biochem. 2007 Sep;303(1-2):183-8. doi: 10.1007/s11010-007-9472-z. Epub 2007 May 9.
Phosphorylation status of RNA polymerase (RNAP) II's largest subunit C-terminal domain (CTD) plays an important role during transcription cycles. The reversible phosphorylation mainly occurs at serine 2 and serine 5 of CTD heptapeptide repeats and regulates RNAP II's activity during transcription initiation, elongation and RNA processing. Here we expressed and characterized HSPC129, a putative human protein bearing a CTD phosphatase domain (CPD). PCR analysis showed that it was ubiquitously expressed. HSPC129DeltaTM, the truncate HSPC129 with first 156 N terminal amino acids deleted, exhibited Mg(2+) dependent phosphatase activity at pH 5.0. Its specific CTD phosphatase activity was verified in vitro. Our research suggests that HSPC129 may regulate the dynamic phosphorylation of RNAP II CTD.
RNA聚合酶（RNAP）II最大亚基的C末端结构域（CTD）的磷酸化状态在转录周期中起着重要作用。可逆磷酸化主要发生在CTD七肽重复序列的丝氨酸2和丝氨酸5处，并在转录起始、延伸和RNA加工过程中调节RNAP II的活性。在此，我们表达并鉴定了HSPC129，一种推定的带有CTD磷酸酶结构域（CPD）的人类蛋白质。PCR分析表明它在各处均有表达。HSPC129DeltaTM是缺失前156个N末端氨基酸的截短型HSPC129，在pH 5.0时表现出Mg(2+)依赖性磷酸酶活性。其特异性CTD磷酸酶活性在体外得到了验证。我们的研究表明，HSPC129可能调节RNAP II CTD的动态磷酸化。
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