Rrp17p Is a Eukaryotic Exonuclease Required for 5′ End Processing of Pre-60S Ribosomal RNA

Marlene Oeffinger, Daniel Zenklusen, Angelica Ferguson, Karen E. Wei, Aziz El Hage, David Tollervey, Brian T. Chait, Robert H. Singer, Michael P. Rout

Research output: Contribution to journalArticlepeer-review

71 Scopus citations


Ribosomal processing requires a series of endo- and exonucleolytic steps for the production of mature ribosomes, of which most have been described. To ensure ribosome synthesis, 3′ end formation of rRNA uses multiple nucleases acting in parallel; however, a similar parallel mechanism had not been described for 5′ end maturation. Here, we identify Rrp17p as a previously unidentified 5′-3′ exonuclease essential for ribosome biogenesis, functioning with Rat1p in a parallel processing pathway analogous to that of 3′ end formation. Rrp17p is required for efficient exonuclease digestion of the mature 5′ ends of 5.8SS and 25S rRNAs, contains a catalytic domain close to its N terminus, and is highly conserved among higher eukaryotes, being a member of a family of exonucleases. We show that Rrp17p binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery, and provide evidence for physical and functional links between late 60S subunit processing and export.

Original languageEnglish (US)
Pages (from-to)768-781
Number of pages14
JournalMolecular Cell
Issue number5
StatePublished - Dec 11 2009


  • RNA

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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