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

Author

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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
    Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke)

  • Benoit Coulombe

    (Translational Proteomics Laboratory, Institut de Recherches Cliniques de Montréal (IRCM)
    Université de Montréal)

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.

Suggested Citation

  • Philippe Cloutier & Christian Poitras & Mathieu Durand & Omid Hekmat & Émilie Fiola-Masson & Annie Bouchard & Denis Faubert & Benoit Chabot & Benoit Coulombe, 2017. "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein," Nature Communications, Nature, vol. 8(1), pages 1-14, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15615
    DOI: 10.1038/ncomms15615
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    Cited by:

    1. Carlos Company & Matthias Jürgen Schmitt & Yuliia Dramaretska & Michela Serresi & Sonia Kertalli & Ben Jiang & Jiang-An Yin & Adriano Aguzzi & Iros Barozzi & Gaetano Gargiulo, 2024. "Logical design of synthetic cis-regulatory DNA for genetic tracing of cell identities and state changes," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    2. Hui Wang & Boyuan Li & Linyu Zuo & Bo Wang & Yan Yan & Kai Tian & Rong Zhou & Chenlu Wang & Xizi Chen & Yongpeng Jiang & Haonan Zheng & Fangfei Qin & Bin Zhang & Yang Yu & Chao-Pei Liu & Yanhui Xu & J, 2022. "The transcriptional coactivator RUVBL2 regulates Pol II clustering with diverse transcription factors," Nature Communications, Nature, vol. 13(1), pages 1-26, December.

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