Synergistic defect in 60S ribosomal subunit assembly caused by a mutation of Rrs1p, a ribosomal protein L11-binding protein, and 3′-extension of 5S rRNA in Saccharomyces cerevisiae

被引:31
作者
Nariai, M [1 ]
Tanaka, T [1 ]
Okada, T [1 ]
Shirai, C [1 ]
Horigome, C [1 ]
Mizuta, K [1 ]
机构
[1] Hiroshima Univ, Grad Sch Biosphere Sci, Dept Bioresource Sci & Technol, Higashihiroshima 7398528, Japan
基金
日本学术振兴会;
关键词
D O I
10.1093/nar/gki772
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
Rrs1p, a ribosomal protein L11-binding protein, has an essential role in biogenesis of 60S ribosomal subunits. We obtained conditionally synthetic lethal allele with the rrs1-5 mutation and determined that the mutation is in REX1, which encodes an exonuclease. The highly conserved leucine at 305 was substituted with tryptophan in rex1-1. The rex1-1 allele resulted in 3'-extended 5S rRNA. Polysome analysis revealed that rex1-1 and rrs1-5 caused a synergistic defect in the assembly of 60S ribosomal subunits. In vivo and in vitro binding assays indicate that Rrs1p interacts with the ribosomal protein L5-5S rRNA complex. The rrs1-5 mutation weakens the interaction between Rrs1p with both L5 and L11. These data suggest that the assembly of L5-5S rRNA on 60S ribosomal subunits coordinates with assembly of L11 via Rrs1p.
引用
收藏
页码:4553 / 4562
页数:10
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