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


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 5.8S(S) 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
Pages (from-to)768-781
Number of pages14
JournalMolecular Cell
Issue number5
Publication statusPublished - 11 Dec 2009


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