An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae

Michael S. Kobor, Jacques Archambault, William Lester, Frank C.P. Holstege, Opher Gileadi, David B. Jansma, Ezra G. Jennings, Fiona Kouyoumdjian, Alan R. Davidson, Richard A. Young, Jack Greenblatt

Research output: Contribution to journalArticlepeer-review

171 Citations (Scopus)

Abstract

The carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II is phosphorylated soon after transcriptional initiation. We show here that the essential FCP1 gene of S. cerevisiae is linked genetically to RNA polymerase II and encodes a CTD phosphatase essential for dephosphorylation of RNA polymerase II in vivo. Fcp1p contains a phosphatase motif, ψψψ DXDX(T/V)ψψ, which is novel for eukaryotic protein phosphatases and essential for Fcp1p to function in vivo. This motif is also required for recombinant Fcp1p to dephosphorylate the RNA polymerase II CTD or the artificial substrate p-nitrophenylphosphate in vitro. The effects of fcp1 mutations in global run-on and genome-wide expression studies show that transcription by RNA polymerase II in S. cerevisiae generally requires CTD phosphatase.

Original languageEnglish
Pages (from-to)55-62
Number of pages8
JournalMolecular Cell
Volume4
Issue number1
DOIs
Publication statusPublished - Jul 1999
Externally publishedYes

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