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Rrp8p is a yeast nucleolar protein functionally linked to Gar1p and involved in pre-rRNA cleavage at site A2

Published online by Cambridge University Press:  01 June 2000

CÉCILE BOUSQUET-ANTONELLI
Affiliation:
Laboratoire de Biologie Moléculaire Eucaryote du Centre National de la Recherche Scientifique, 31062 Toulouse Cedex 04, France Present address: Institute of Cell and Molecular Biology, University of Edinburgh, King's Buildings, Edinburgh EH9 3JR, United Kingdom.
EMMANUEL VANROBAYS
Affiliation:
Laboratoire de Biologie Moléculaire Eucaryote du Centre National de la Recherche Scientifique, 31062 Toulouse Cedex 04, France
JEAN-PAUL GÉLUGNE
Affiliation:
Laboratoire de Biologie Moléculaire Eucaryote du Centre National de la Recherche Scientifique, 31062 Toulouse Cedex 04, France
MICHÈLE CAIZERGUES-FERRER
Affiliation:
Laboratoire de Biologie Moléculaire Eucaryote du Centre National de la Recherche Scientifique, 31062 Toulouse Cedex 04, France
YVES HENRY
Affiliation:
Laboratoire de Biologie Moléculaire Eucaryote du Centre National de la Recherche Scientifique, 31062 Toulouse Cedex 04, France
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Abstract

Chemical modifications and processing of the 18S, 5.8S, and 25S ribosomal RNAs from the 35S pre-ribosomal RNA depend on an important set of small nucleolar ribonucleoprotein particles (snoRNPs). Genetic depletion of yeast Gar1p, an essential common component of H/ACA snoRNPs, leads to inhibition of uridine isomerizations to pseudouridines on the 35S pre-rRNA and of the early pre-rRNA cleavages at sites A1 and A2, resulting in a loss of mature 18S rRNA synthesis. To identify Gar1p functional partners, we screened for mutations that are synthetically lethal with a gar1 mutant allele encoding a Gar1p mutant protein lacking its two glycine/arginine-rich (GAR) domains. We identified a previously uncharacterized Saccharomyces cerevisiae open reading frame, YDR083W (now designated RRP8), that encodes a highly conserved protein containing motifs found in methyltransferases. Rrp8p localizes to the nucleolus. A yeast strain lacking this protein is viable at 30 °C but displays strong growth impairment at lower temperatures. In this strain, cleavage of the pre-rRNA at site A2 is strongly affected whereas cleavages at sites A0 and A1 are only slightly inhibited or delayed.

Type
Research Article
Copyright
2000 RNA Society

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