Title: R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein (2017)

Authors: Philippe Cloutier, Christian Poitras, Mathieu Durand, Omid Hekmat, Émilie Fiola-Masson, Annie Bouchard, Denis Faubert, Benoit Chabot and Benoit Coulombe

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. This article reports 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 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 is shown to impact 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.

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• Table S1 is a number of TAP purifications with interactors that were selected based on a very stringent specificity threshold score calculated by DECONTAMINATOR.
• Table S2 is a single BioID experiment where false discovery rates have been calculated instead by SAINT.