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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Feng Y,Kang JS,Kim S,Yun DJ,Lee SY,Bahk JD,Koiwa H

doi

10.1016/j.bbrc.2010.05.130

subject

Has Abstract

pub_date

2010-06-25 00:00:00

pages

355-60

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(10)01045-4

journal_volume

397

pub_type

杂志文章

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