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

被引:37
作者
Bousquet-Antonelli, C [1 ]
Vanrobays, E [1 ]
Gélugne, JP [1 ]
Caizergues-Ferrer, M [1 ]
Henry, Y [1 ]
机构
[1] CNRS, Lab Biol Mol Eucaryote, F-31062 Toulouse 04, France
关键词
GAR domain; methyltransferase; pre-rRNA processing; Saccharomyces cerevisiae; synthetic lethal screen; YDR083W;
D O I
10.1017/S1355838200992288
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Chemical modifications and processing of the 18S, 5.8S, and 25S ribosomai RNAs from the 355 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 355 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 degrees 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.
引用
收藏
页码:826 / 843
页数:18
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