Molecular and Cellular Biochemistry

, Volume 303, Issue 1, pp 183–188

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

  • Hui Qian
  • Chaoneng Ji
  • Shuo Zhao
  • Jinzhong Chen
  • Mei Jiang
  • Yong Zhang
  • Mi Yan
  • Dan Zheng
  • Yaqiong Sun
  • Yi Xie
  • Yumin Mao
Article

DOI: 10.1007/s11010-007-9472-z

Cite this article as:
Qian, H., Ji, C., Zhao, S. et al. Mol Cell Biochem (2007) 303: 183. doi:10.1007/s11010-007-9472-z

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. HSPC129ΔTM, the truncate HSPC129 with first 156 N terminal amino acids deleted, exhibited Mg2+ 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.

Keywords

HSPC129 CTDSPL2 RNA polymerase II Dephosphorylation CTD phosphatase 

Copyright information

© Springer Science+Business Media, LLC 2007

Authors and Affiliations

  • Hui Qian
    • 1
  • Chaoneng Ji
    • 1
  • Shuo Zhao
    • 1
  • Jinzhong Chen
    • 1
  • Mei Jiang
    • 1
  • Yong Zhang
    • 1
  • Mi Yan
    • 1
  • Dan Zheng
    • 1
  • Yaqiong Sun
    • 1
  • Yi Xie
    • 1
  • Yumin Mao
    • 1
  1. 1.State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life SciencesFudan UniversityShanghaiP.R. China

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