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

Authors
  • Elela, S A
  • Igel, H
  • Ares, M Jr
Type
Published Article
Journal
Cell
Publisher
Elsevier
Publication Date
Apr 05, 1996
Volume
85
Issue
1
Pages
115–124
Identifiers
PMID: 8620530
Source
Medline
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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