R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein

Philippe Cloutier, Christian Poitras, Mathieu Durand, Omid Hekmat, Émilie Fiola-Masson, Annie Bouchard, Denis Faubert, Benoit Chabot and Benoit Coulombe ()
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Philippe Cloutier: Translational Proteomics Laboratory, Institut de Recherches Cliniques de Montréal (IRCM)
Christian Poitras: Translational Proteomics Laboratory, Institut de Recherches Cliniques de Montréal (IRCM)
Mathieu Durand: Laboratory of Functional Genomics, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke
Omid Hekmat: Translational Proteomics Laboratory, Institut de Recherches Cliniques de Montréal (IRCM)
Émilie Fiola-Masson: Translational Proteomics Laboratory, Institut de Recherches Cliniques de Montréal (IRCM)
Annie Bouchard: Translational Proteomics Laboratory, Institut de Recherches Cliniques de Montréal (IRCM)
Denis Faubert: Translational Proteomics Laboratory, Institut de Recherches Cliniques de Montréal (IRCM)
Benoit Chabot: Laboratory of Functional Genomics, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke
Benoit Coulombe: Translational Proteomics Laboratory, Institut de Recherches Cliniques de Montréal (IRCM)

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: Abstract The R2TP/Prefoldin-like (R2TP/PFDL) complex has emerged as a cochaperone complex involved in the assembly of a number of critical protein complexes including snoRNPs, nuclear RNA polymerases and PIKK-containing complexes. Here we report on the use of multiple target affinity purification coupled to mass spectrometry to identify two additional complexes that interact with R2TP/PFDL: the TSC1–TSC2 complex and the U5 small nuclear ribonucleoprotein (snRNP). The interaction between R2TP/PFDL and the U5 snRNP is mostly mediated by the previously uncharacterized factor ZNHIT2. A more general function for the zinc-finger HIT domain in binding RUVBL2 is exposed. Disruption of ZNHIT2 and RUVBL2 expression impacts the protein composition of the U5 snRNP suggesting a function for these proteins in promoting the assembly of the ribonucleoprotein. A possible implication of R2TP/PFDL as a major effector of stress-, energy- and nutrient-sensing pathways that regulate anabolic processes through the regulation of its chaperoning activity is discussed.

Date: 2017
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DOI: 10.1038/ncomms15615

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