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

Rockefeller University, New York, NY 10065, USA.
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.
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
Mol. Cell Dec. 11, 2009; 36(5);768-81 [PUBMED:20005841]
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