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rdf:type |
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lifeskim:mentions |
umls-concept:C0014442,
umls-concept:C0033684,
umls-concept:C0040649,
umls-concept:C0086418,
umls-concept:C0220922,
umls-concept:C0302167,
umls-concept:C0337076,
umls-concept:C0936012,
umls-concept:C1419400,
umls-concept:C1704675,
umls-concept:C1882071,
umls-concept:C2003939
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pubmed:issue |
2
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pubmed:dateCreated |
2007-7-23
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pubmed:abstractText |
We have performed a survey of soluble human protein complexes containing components of the transcription and RNA processing machineries using protein affinity purification coupled to mass spectrometry. Thirty-two tagged polypeptides yielded a network of 805 high-confidence interactions. Remarkably, the network is significantly enriched in proteins that regulate the formation of protein complexes, including a number of previously uncharacterized proteins for which we have inferred functions. The RNA polymerase II (RNAP II)-associated proteins (RPAPs) are physically and functionally associated with RNAP II, forming an interface between the enzyme and chaperone/scaffolding proteins. BCDIN3 is the 7SK snRNA methylphosphate capping enzyme (MePCE) present in an snRNP complex containing both RNA processing and transcription factors, including the elongation factor P-TEFb. Our results define a high-density protein interaction network for the mammalian transcription machinery and uncover multiple regulatory factors that target the transcription machinery.
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pubmed:commentsCorrections |
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1097-2765
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pubmed:author |
pubmed-author:BergeronDominiqueD,
pubmed-author:BlanchetteMathieuM,
pubmed-author:BouchardAnnieA,
pubmed-author:BourassaSylvieS,
pubmed-author:ChabotBenoitB,
pubmed-author:ChuaGordonG,
pubmed-author:CoulombeBenoitB,
pubmed-author:ForgetDianeD,
pubmed-author:GreenblattJackJ,
pubmed-author:HughesTimothy RTR,
pubmed-author:JeronimoCéliaC,
pubmed-author:LiQintongQ,
pubmed-author:PoirierGuy GGG,
pubmed-author:PoitrasChristianC,
pubmed-author:PriceDavid HDH,
pubmed-author:ThérienCynthiaC
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
262-74
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pubmed:dateRevised |
2007-9-12
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pubmed:meshHeading |
pubmed-meshheading:17643375-Amino Acid Sequence,
pubmed-meshheading:17643375-Carrier Proteins,
pubmed-meshheading:17643375-Cell Line,
pubmed-meshheading:17643375-Humans,
pubmed-meshheading:17643375-Macromolecular Substances,
pubmed-meshheading:17643375-Molecular Sequence Data,
pubmed-meshheading:17643375-Nucleotidyltransferases,
pubmed-meshheading:17643375-Protein Interaction Mapping,
pubmed-meshheading:17643375-RNA Interference,
pubmed-meshheading:17643375-RNA Polymerase II,
pubmed-meshheading:17643375-RNA Processing, Post-Transcriptional,
pubmed-meshheading:17643375-Ribonucleoproteins, Small Nuclear,
pubmed-meshheading:17643375-Transcription, Genetic
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pubmed:year |
2007
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pubmed:articleTitle |
Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme.
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pubmed:affiliation |
Laboratory of Gene Transcription and Proteomics Discovery Platform, Institut de Recherches Cliniques de Montréal, Montréal, QC, Canada.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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