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

François Dragon, 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, Susan J. Baserga

Research output: Contribution to journalArticlepeer-review

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 ago, 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 tested. Biochemical and genetic analyses suggest that U3-pre-rRNA base-pairing interactions mediate endonucleolytic pre-rRNA cleavages. Here we have purified a large ribonudeoprotein (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.

Original languageEnglish (US)
Pages (from-to)967-970
Number of pages4
JournalNature
Volume417
Issue number6892
DOIs
StatePublished - 2002

ASJC Scopus subject areas

  • General

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