Arabidopsis SCP1-like small phosphatases differentially dephosphorylate RNA polymerase II C-terminal domain. Academic Article uri icon


  • RNA polymerase II carboxyl-terminal domain (pol II CTD) phosphatases that can dephosphorylate both Ser2-PO(4) and Ser5-PO(4) of CTD have been identified in animals and yeasts, however, only Ser5-PO(4)-specific CTD phosphatases have been identified in plants. Among predicted Arabidopsis SCP1-like small phosphatases (SSP), SSP4, SSP4b, and SSP5 form a unique group with long N-terminal extensions. While SSPs' expression showed similar tissue-specificities, SSP4 and SSP4b were localized exclusively in the nuclei, whereas SSP5 accumulated in both nuclei and cytoplasm. Detailed characterization of SSP activities using various peptides and full-length Arabidopsis pol II CTD substrates established that SSP4 and SSP4b could dephosphorylate both Ser2-PO(4) and Ser5-PO(4) of CTD, whereas SSP5 dephosphorylated only Ser5-PO(4). These results indicate that Arabidopsis SSP gene family encodes active CTD phosphatases like animal SCP1 family proteins, with distinct substrate specificities.

published proceedings

  • Biochem Biophys Res Commun

author list (cited authors)

  • Feng, Y., Kang, J. S., Kim, S., Yun, D. J., Lee, S. Y., Bahk, J. D., & Koiwa, H.

citation count

  • 10

complete list of authors

  • Feng, Yue||Kang, Jae Sook||Kim, Sewon||Yun, Dae Jin||Lee, Sang Yeol||Bahk, Jeong Dong||Koiwa, Hisashi

publication date

  • January 2010