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Mol Cell Biochem. 2007 Sep;303(1-2):183-8. Epub 2007 May 9.

Expression and characterization of HSPC129, a RNA polymerase II C-terminal domain phosphatase.

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State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Room 602, Science Building, Shanghai, PR China.


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.

[Indexed for MEDLINE]

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