Abstract
RNA polymerase II (RNAP II) C-terminal domain (CTD) phosphorylation is important for various transcription-related processes. Here, we identify by affinity purification and mass spectrometry three previously uncharacterized human CTD-interaction domain (CID)-containing proteins, RPRD1A, RPRD1B and RPRD2, which co-purify with RNAP II and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. RPRD1A and RPRD1B can accompany RNAP II from promoter regions to 3'-untranslated regions during transcription in vivo, predominantly interact with phosphorylated RNAP II, and can reduce CTD S5- and S7-phosphorylated RNAP II at target gene promoters. Thus, the RPRD proteins are likely to have multiple important roles in transcription.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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3' Untranslated Regions
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Carrier Proteins / metabolism
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Cell Cycle Proteins / chemistry
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Cell Cycle Proteins / genetics
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Cell Cycle Proteins / metabolism*
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HEK293 Cells
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Humans
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Neoplasm Proteins / chemistry
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Neoplasm Proteins / genetics
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Neoplasm Proteins / metabolism*
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Phosphorylation
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Promoter Regions, Genetic*
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Protein Interaction Domains and Motifs
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RNA Polymerase II / chemistry
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RNA Polymerase II / genetics
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RNA Polymerase II / metabolism*
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RecQ Helicases / metabolism
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Repressor Proteins / chemistry
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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Transcription, Genetic
Substances
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3' Untranslated Regions
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Carrier Proteins
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Cell Cycle Proteins
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Neoplasm Proteins
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POLR2M protein, human
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RECQL5 protein, human
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RPAP2 protein, human
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RPRD1A protein, human
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RPRD1B protein, human
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Repressor Proteins
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RNA Polymerase II
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RecQ Helicases