Abstract
The C-terminal domain (CTD) of Rpb1, the largest subunit of RNA polymerase II, acts as a binding platform for various mRNA processing and histone-modifying enzymes that act co-transcriptionally. These factors are targeted to specific phosphorylation states of the CTD that predominate at different stages of transcription. Within the repeating sequence YSPTSPS, serines 2 and 5 are major phosphorylation sites, but serine 7 phosphorylation was recently discovered in mammalian cells. Here we show that CTD serine 7 is also phosphorylated in yeast and that Ser-7(P) chromatin immunoprecipitation patterns resemble those of Ser-5(P). The basal factor TFIIH can phosphorylate Ser-7 in vitro and is necessary for Ser-7(P) in vivo. Interestingly, deletion of the CTD Ser-5(P) phosphatase Rtr1 leads to an increase in Ser-5(P) but not Ser-7(P).
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Chromatin Immunoprecipitation
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Immunoblotting
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Mutation
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Phosphorylation
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Protein Subunits / genetics
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Protein Subunits / metabolism
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RNA Polymerase II / genetics
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RNA Polymerase II / metabolism*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Serine / genetics
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Serine / metabolism*
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Transcription Factor TFIIH / genetics
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Transcription Factor TFIIH / metabolism
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Transcription Factors / genetics
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Transcription Factors / metabolism
Substances
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Protein Subunits
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Rtr1 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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Transcription Factor TFIIH
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Serine
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RNA Polymerase II
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RPB1 protein, S cerevisiae