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Rrp17p is a eukaryotic exonuclease required for 5' end processing of Pre-60S ribosomal RNA.

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.

Pubmed ID: 20005841

Authors

  • Oeffinger M
  • Zenklusen D
  • Ferguson A
  • Wei KE
  • El Hage A
  • Tollervey D
  • Chait BT
  • Singer RH
  • Rout MP

Journal

Molecular cell

Publication Data

December 11, 2009

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM57071
  • Agency: NIGMS NIH HHS, Id: R01 GM057071
  • Agency: NIGMS NIH HHS, Id: R01 GM062427
  • Agency: NCRR NIH HHS, Id: RR00862
  • Agency: NCRR NIH HHS, Id: RR022220
  • Agency: Wellcome Trust, Id:

Mesh Terms

  • Amino Acid Sequence
  • Exonucleases
  • Exoribonucleases
  • Humans
  • Membrane Proteins
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • RNA Precursors
  • RNA Processing, Post-Transcriptional
  • RNA, Ribosomal
  • Ribosomes
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment