The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation Journal Article


Authors: Friedl, E. M.; Lane, W. S.; Erdjument-Bromage, H.; Tempst, P.; Reinberg, D.
Article Title: The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation
Abstract: The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (RNAPII) is heavily phosphorylated during the transition from transcription initiation to the establishment of an elongation-competent transcription complex. FCP1 is the only phosphatase known to be specific for the CTD of the largest subunit of RNAPII, and its activity is believed to be required to reactivate RNAPII, so that RNAPII can enter another round of transcription. We demonstrate that FCP1 is a phosphoprotein, and that phosphorylation regulates FCP1 activities. FCP1 is phosphorylated at multiple sites in vivo. The CTD phosphatase activity of phosphorylated FCP1 is stimulated by TFIIF, whereas dephosphorylated FCP1 is not. In addition to its role in the recycling of RNAPII, FCP1 also affects transcription elongation. Phosphorylated FCP1 is more active in stimulating transcription elongation than the dephosphorylated form of FCP1. We found that only phosphorylated FCP1 can physically interact with TFIIF. We set out to purify an FCP1 kinase from HeLa cells and identified casein kinase 2, which, surprisingly, displayed a negative effect on FCP1-associated activities.
Keywords: unclassified drug; human cell; animals; carboxy terminal sequence; cell line; transcription, genetic; enzyme activity; hela cell; hela cells; phosphorylation; gene expression regulation; alkaline phosphatase; blotting, western; enzyme phosphorylation; transcription regulation; molecular sequence data; protein-serine-threonine kinases; base sequence; protein structure, tertiary; cell nucleus; protein kinase; rna polymerase ii; phosphoprotein phosphatase; insects; baculoviridae; casein kinase ii; precipitin tests; protein fcp1; humans; human; priority journal; article; fcp1 kinase
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 100
Issue: 5
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2003-03-04
Start Page: 2328
End Page: 2333
Language: English
DOI: 10.1073/pnas.2628049100
PUBMED: 12591939
PROVIDER: scopus
PMCID: PMC151340
DOI/URL:
Notes: Export Date: 12 September 2014 -- Source: Scopus
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  1. Paul J Tempst
    324 Tempst