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  • Title: Expression and characterization of HSPC129, a RNA polymerase II C-terminal domain phosphatase.
    Author: Qian H, Ji C, Zhao S, Chen J, Jiang M, Zhang Y, Yan M, Zheng D, Sun Y, Xie Y, Mao Y.
    Journal: Mol Cell Biochem; 2007 Sep; 303(1-2):183-8. PubMed ID: 17487459.
    Abstract:
    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.
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