Abstract
The largest subunit of the human basal transcription factor TFIIFalpha (also called RAP74) was reported previously to be the target of some phospho/dephosphorylation process. We show that TFIIFalpha possesses a serine/threonine kinase activity, allowing an autophosphorylation of the two residues at position serine 385 and threonine 389. Mutation analysis strongly suggests that autophosphorylation of both sites regulates the transcription elongation process. Moreover we also evidence three additional phosphorylation sites located at positions 207-230, 271-283, and 335-344. These sites are phosphorylated by casein kinase II-like kinases and TAF(II)250, a component of TFIID.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Casein Kinase II
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DNA Mutational Analysis
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DNA-Binding Proteins / metabolism
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Histone Acetyltransferases
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Humans
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Molecular Sequence Data
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Nuclear Proteins / metabolism
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Phosphorylation
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Recombinant Proteins / metabolism
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Spodoptera / genetics
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Substrate Specificity
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TATA-Binding Protein Associated Factors*
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Transcription Factor TFIID
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription Factors, TFII / metabolism
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Transcription, Genetic*
Substances
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DNA-Binding Proteins
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Nuclear Proteins
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Recombinant Proteins
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TATA-Binding Protein Associated Factors
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Transcription Factor TFIID
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Transcription Factors
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Transcription Factors, TFII
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Histone Acetyltransferases
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Casein Kinase II
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Protein Serine-Threonine Kinases
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TATA-binding protein associated factor 250 kDa
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transcription factor TFIIF