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rdf:type |
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lifeskim:mentions |
umls-concept:C0031715,
umls-concept:C0035679,
umls-concept:C0076920,
umls-concept:C0108555,
umls-concept:C1149880,
umls-concept:C1167622,
umls-concept:C1333721,
umls-concept:C1333722,
umls-concept:C1413790,
umls-concept:C1415343,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2349975
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pubmed:issue |
39
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pubmed:dateCreated |
2002-9-23
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinase II,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sepharose,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, TFII,
http://linkedlifedata.com/resource/pubmed/chemical/carboxy-terminal domain phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/transcription factor TFIIF
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36061-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12138108-Amino Acid Sequence,
pubmed-meshheading:12138108-Animals,
pubmed-meshheading:12138108-Blotting, Western,
pubmed-meshheading:12138108-Casein Kinase II,
pubmed-meshheading:12138108-Chromatography,
pubmed-meshheading:12138108-Dose-Response Relationship, Drug,
pubmed-meshheading:12138108-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12138108-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:12138108-Glutathione,
pubmed-meshheading:12138108-Molecular Sequence Data,
pubmed-meshheading:12138108-Phosphoprotein Phosphatases,
pubmed-meshheading:12138108-Phosphoproteins,
pubmed-meshheading:12138108-Phosphorylation,
pubmed-meshheading:12138108-Plasmids,
pubmed-meshheading:12138108-Precipitin Tests,
pubmed-meshheading:12138108-Protein Binding,
pubmed-meshheading:12138108-Protein Phosphatase 1,
pubmed-meshheading:12138108-Protein Structure, Tertiary,
pubmed-meshheading:12138108-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12138108-RNA Polymerase II,
pubmed-meshheading:12138108-Recombinant Proteins,
pubmed-meshheading:12138108-Sepharose,
pubmed-meshheading:12138108-Serine,
pubmed-meshheading:12138108-Time Factors,
pubmed-meshheading:12138108-Transcription, Genetic,
pubmed-meshheading:12138108-Transcription Factors, TFII,
pubmed-meshheading:12138108-Xenopus,
pubmed-meshheading:12138108-Xenopus laevis
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pubmed:year |
2002
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pubmed:articleTitle |
FCP1 phosphorylation by casein kinase 2 enhances binding to TFIIF and RNA polymerase II carboxyl-terminal domain phosphatase activity.
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pubmed:affiliation |
UMR 8541 CNRS, Génétique Moléculaire, Ecole Normale Supérieure, 46 rue d'Ulm, 75230 Paris Cedex 05, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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