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A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis

Author

Listed:
  • François Dragon

    (Yale University School of Medicine
    Université du Québec à Montréal)

  • Jennifer E. G. Gallagher

    (Yale University School of Medicine)

  • Patricia A. Compagnone-Post

    (Yale University School of Medicine)

  • Brianna M. Mitchell

    (Yale University School of Medicine)

  • Kara A. Porwancher

    (Yale University School of Medicine)

  • Karen A. Wehner

    (Yale University School of Medicine)

  • Steven Wormsley

    (Yale University School of Medicine)

  • Robert E. Settlage

    (ProteoMS, LLC)

  • Jeffrey Shabanowitz

    (University of Virginia)

  • Yvonne Osheim

    (University of Virginia)

  • Ann L. Beyer

    (University of Virginia)

  • Donald F. Hunt

    (University of Virginia
    University of Virginia)

  • Susan J. Baserga

    (Yale University School of Medicine
    Yale University School of Medicine)

Abstract

Although the U3 small nucleolar RNA (snoRNA), a member of the box C/D class of snoRNAs, was identified with the spliceosomal small nuclear RNAs (snRNAs) over 30 years ago1,2, its function and its associated protein components have remained more elusive. The U3 snoRNA is ubiquitous in eukaryotes and is required for nucleolar processing of pre-18S ribosomal RNA in all organisms where it has been tested3,4. Biochemical and genetic analyses suggest that U3–pre-rRNA base-pairing interactions mediate endonucleolytic pre-rRNA cleavages3. Here we have purified a large ribonucleoprotein (RNP) complex from Saccharomyces cerevisiae that contains the U3 snoRNA and 28 proteins. Seventeen new proteins (Utp1–17) and Rrp5 were present, as were ten known components. The Utp proteins are nucleolar and specifically associated with the U3 snoRNA. Depletion of the Utp proteins impedes production of the 18S rRNA, indicating that they are part of the active pre-rRNA processing complex. On the basis of its large size (80S; calculated relative molecular mass of at least 2,200,000) and function, this complex may correspond to the terminal knobs present at the 5′ ends of nascent pre-rRNAs. We have termed this large RNP the small subunit (SSU) processome.

Suggested Citation

  • François Dragon & Jennifer E. G. Gallagher & Patricia A. Compagnone-Post & Brianna M. Mitchell & Kara A. Porwancher & Karen A. Wehner & Steven Wormsley & Robert E. Settlage & Jeffrey Shabanowitz & Yvo, 2002. "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis," Nature, Nature, vol. 417(6892), pages 967-970, June.
    • Handle: RePEc:nat:nature:v:417:y:2002:i:6892:d:10.1038_nature00769
    DOI: 10.1038/nature00769
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    Cited by:

    1. Gerald Ryan R. Aquino & Philipp Hackert & Nicolai Krogh & Kuan-Ting Pan & Mariam Jaafar & Anthony K. Henras & Henrik Nielsen & Henning Urlaub & Katherine E. Bohnsack & Markus T. Bohnsack, 2021. "The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    2. Konstantin Axt & Sarah L French & Ann L Beyer & David Tollervey, 2014. "Kinetic Analysis Demonstrates a Requirement for the Rat1 Exonuclease in Cotranscriptional Pre-rRNA Cleavage," PLOS ONE, Public Library of Science, vol. 9(2), pages 1-11, February.

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