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UtpA and UtpB chaperone nascent pre-ribosomal RNA and U3 snoRNA to initiate eukaryotic ribosome assembly

Author

Listed:
  • Mirjam Hunziker

    (Laboratory of Protein and Nucleic Acid Chemistry, The Rockefeller University)

  • Jonas Barandun

    (Laboratory of Protein and Nucleic Acid Chemistry, The Rockefeller University)

  • Elisabeth Petfalski

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Max Born Crescent)

  • Dongyan Tan

    (Harvard Medical School)

  • Clémentine Delan-Forino

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Max Born Crescent)

  • Kelly R. Molloy

    (Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University)

  • Kelly H. Kim

    (Laboratory of Molecular Electron Microscopy, The Rockefeller University)

  • Hywel Dunn-Davies

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Max Born Crescent)

  • Yi Shi

    (Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University)

  • Malik Chaker-Margot

    (Laboratory of Protein and Nucleic Acid Chemistry, The Rockefeller University
    Tri-Institutional Training Program in Chemical Biology, The Rockefeller University)

  • Brian T. Chait

    (Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University)

  • Thomas Walz

    (Laboratory of Molecular Electron Microscopy, The Rockefeller University)

  • David Tollervey

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Max Born Crescent)

  • Sebastian Klinge

    (Laboratory of Protein and Nucleic Acid Chemistry, The Rockefeller University)

Abstract

Early eukaryotic ribosome biogenesis involves large multi-protein complexes, which co-transcriptionally associate with pre-ribosomal RNA to form the small subunit processome. The precise mechanisms by which two of the largest multi-protein complexes—UtpA and UtpB—interact with nascent pre-ribosomal RNA are poorly understood. Here, we combined biochemical and structural biology approaches with ensembles of RNA–protein cross-linking data to elucidate the essential functions of both complexes. We show that UtpA contains a large composite RNA-binding site and captures the 5′ end of pre-ribosomal RNA. UtpB forms an extended structure that binds early pre-ribosomal intermediates in close proximity to architectural sites such as an RNA duplex formed by the 5′ ETS and U3 snoRNA as well as the 3′ boundary of the 18S rRNA. Both complexes therefore act as vital RNA chaperones to initiate eukaryotic ribosome assembly.

Suggested Citation

  • Mirjam Hunziker & Jonas Barandun & Elisabeth Petfalski & Dongyan Tan & Clémentine Delan-Forino & Kelly R. Molloy & Kelly H. Kim & Hywel Dunn-Davies & Yi Shi & Malik Chaker-Margot & Brian T. Chait & Th, 2016. "UtpA and UtpB chaperone nascent pre-ribosomal RNA and U3 snoRNA to initiate eukaryotic ribosome assembly," Nature Communications, Nature, vol. 7(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12090
    DOI: 10.1038/ncomms12090
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    Cited by:

    1. Nic Robertson & Vadim Shchepachev & David Wright & Tomasz W. Turowski & Christos Spanos & Aleksandra Helwak & Rose Zamoyska & David Tollervey, 2022. "A disease-linked lncRNA mutation in RNase MRP inhibits ribosome synthesis," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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