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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5673
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pubmed:dateCreated |
2004-5-14
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pubmed:abstractText |
Dynamic changes in chromatin structure, induced by posttranslational modification of histones, play a fundamental role in regulating eukaryotic transcription. Here we report that histone H2B is phosphorylated at evolutionarily conserved Ser33 (H2B-S33) by the carboxyl-terminal kinase domain (CTK) of the Drosophila TFIID subunit TAF1. Phosphorylation of H2B-S33 at the promoter of the cell cycle regulatory gene string and the segmentation gene giant coincides with transcriptional activation. Elimination of TAF1 CTK activity in Drosophila cells and embryos reduces transcriptional activation and phosphorylation of H2B-S33. These data reveal that H2B-S33 is a physiological substrate for the TAF1 CTK and that H2B-S33 phosphorylation is essential for transcriptional activation events that promote cell cycle progression and development.
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pubmed:grant |
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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/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Taf1 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/caudal protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/giant protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/stg protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
14
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pubmed:volume |
304
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1010-4
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15143281-Acetylation,
pubmed-meshheading:15143281-Amino Acid Motifs,
pubmed-meshheading:15143281-Amino Acid Sequence,
pubmed-meshheading:15143281-Amino Acid Substitution,
pubmed-meshheading:15143281-Animals,
pubmed-meshheading:15143281-Cell Cycle,
pubmed-meshheading:15143281-Cell Cycle Proteins,
pubmed-meshheading:15143281-DNA-Binding Proteins,
pubmed-meshheading:15143281-Drosophila,
pubmed-meshheading:15143281-Drosophila Proteins,
pubmed-meshheading:15143281-Embryo, Nonmammalian,
pubmed-meshheading:15143281-Genes, Insect,
pubmed-meshheading:15143281-Histone Acetyltransferases,
pubmed-meshheading:15143281-Histones,
pubmed-meshheading:15143281-Homeodomain Proteins,
pubmed-meshheading:15143281-Molecular Sequence Data,
pubmed-meshheading:15143281-Mutation,
pubmed-meshheading:15143281-Phosphorylation,
pubmed-meshheading:15143281-Phosphoserine,
pubmed-meshheading:15143281-Promoter Regions, Genetic,
pubmed-meshheading:15143281-Protein Structure, Tertiary,
pubmed-meshheading:15143281-Protein Tyrosine Phosphatases,
pubmed-meshheading:15143281-RNA Interference,
pubmed-meshheading:15143281-Recombinant Proteins,
pubmed-meshheading:15143281-Repressor Proteins,
pubmed-meshheading:15143281-Transcription, Genetic,
pubmed-meshheading:15143281-Transcription Factor TFIID,
pubmed-meshheading:15143281-Transcription Factors,
pubmed-meshheading:15143281-Transcriptional Activation
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pubmed:year |
2004
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pubmed:articleTitle |
TAF1 activates transcription by phosphorylation of serine 33 in histone H2B.
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pubmed:affiliation |
Department of Biochemistry, University of California-Riverside, Riverside, CA 95121, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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