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
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