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Systematic Analysis of the Protein Interaction Network for the Human Transcription Machinery Reveals the Identity of the 7SK Capping Enzyme
Journal article   Open access   Peer reviewed

Systematic Analysis of the Protein Interaction Network for the Human Transcription Machinery Reveals the Identity of the 7SK Capping Enzyme

Célia Jeronimo, Diane Forget, Annie Bouchard, Qintong Li, Gordon Chua, Christian Poitras, Cynthia Thérien, Dominique Bergeron, Sylvie Bourassa, Jack Greenblatt, …
Molecular cell, Vol.27(2), pp.262-274
2007
DOI: 10.1016/j.molcel.2007.06.027
PMCID: PMC4498903
PMID: 17643375
url
https://doi.org/10.1016/j.molcel.2007.06.027View
Published (Version of record) Open Access

Abstract

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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