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RNase III cleaves eukaryotic preribosomal RNA at a U3 snoRNP-dependent site.

Authors
  • Sa, Elela
  • H, Igel
  • Jr, Ares M
Type
Published Article
Journal
Cell
Publisher
Elsevier
Volume
85
Issue
1
Pages
115–124
Source
UCSC Bioinformatics biomedical-ucsc
License
Unknown

Abstract

A yeast gene homologous to bacterial RNase III (RNT1) encodes a double-strand-specific endoribonuclease essential for ribosome synthesis. Two rRNA processing events are blocked in cells temperature sensitive for RNT1: cleavage at the snoRNA-dependent AO site in the 5 ETS and cleavage in the 3 ETS. Recombinant RNT1 protein accurately cleaves a synthetic 5 ETS RNA at AO site in vitro, in the absence of snoRNA or other factors. A synthetic 3 ETS substrate is specifically cleaved at a site 21 nt downstream of the 3 end 28S rRNA. These observations show that a protein endonuclease collaborates with snoRNAs in eukaryotic rRNA processing and exclude a catalytic role for snoRNAs at certain pre-rRNA cleavage.

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