A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis
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,
Yvonne Osheim,
Ann L. Beyer,
Donald F. Hunt and
Susan J. Baserga ()
Additional contact information
François Dragon: Yale University School of Medicine
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
Susan J. Baserga: Yale University School of Medicine
Nature, 2002, vol. 417, issue 6892, 967-970
Abstract:
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.
Date: 2002
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DOI: 10.1038/nature00769
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