FCP1 Phosphorylation by Casein Kinase 2 Enhances Binding to TFIIF and RNA Polymerase II Carboxyl-terminal Domain Phosphatase Activity
Autor: | Olivier Bensaude, Benoit Palancade, Marie-Françoise Dubois |
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Rok vydání: | 2002 |
Předmět: |
Time Factors
Transcription Genetic Xenopus Blotting Western Molecular Sequence Data genetic processes RNA polymerase II Protein Serine-Threonine Kinases environment and public health Biochemistry Gene Expression Regulation Enzymologic Transcription Factors TFII Xenopus laevis Protein Phosphatase 1 Casein kinase 2 alpha 1 Phosphoprotein Phosphatases Serine Animals Amino Acid Sequence Phosphorylation Casein Kinase II Molecular Biology RNA polymerase II holoenzyme Chromatography Dose-Response Relationship Drug biology Sepharose fungi Cell Biology Phosphoproteins Glutathione Precipitin Tests Recombinant Proteins Protein Structure Tertiary enzymes and coenzymes (carbohydrates) health occupations biology.protein Electrophoresis Polyacrylamide Gel Cyclin-dependent kinase 9 Transcription factor II F RNA Polymerase II CTD phosphatase activity Transcription factor II D Transcription factor II B Plasmids Protein Binding |
Zdroj: | Journal of Biological Chemistry. 277:36061-36067 |
ISSN: | 0021-9258 |
DOI: | 10.1074/jbc.m205192200 |
Popis: | Dephosphorylation of RNA polymerase II carboxyl-terminal domain (CTD) is required to resume sequential transcription cycles. FCP1 (TFIIF-dependent CTD phosphatase 1) is the only known phosphatase targeting RNAP II CTD. Here we show that in Xenopus laevis cells, xFCP1 is a phosphoprotein. On the basis of biochemical fractionation and drug sensitivity, casein kinase 2 (CK2) is shown to be the major kinase involved in xFCP1 phosphorylation in X. laevis egg extracts. CK2 phosphorylates xFCP1 mainly at a cluster of serines centered on Ser(457). CK2-dependent phosphorylation enhances 4-fold the CTD phosphatase activity of FCP1 and its binding to the RAP74 subunit of general transcription factor TFIIF. These findings unravel a new mechanism regulating CTD phosphorylation and hence class II gene transcription. |
Databáze: | OpenAIRE |
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