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

abstract

• 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.

authors

• Koiwa, Hisashi

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

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Arabidopsis
• Arabidopsis Proteins
• Computational Biology
• Phosphoprotein Phosphatases
• Phosphorylation
• Protein Isoforms
• Protein Structure, Tertiary
• RNA Polymerase II
• Serine
• Substrate Specificity

Digital Object Identifier (DOI)

• 10.1016/j.bbrc.2010.05.130

start page

• 355

end page

• 360

volume

• 397

issue

• 2

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.bbrc.2010.05.130