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

Masanobu Nariai, Tomohisa Tanaka, Takafumi Okada, Chiharu Shirai, Chihiro Horigome, Keiko Mizuta

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)4553-4562
Number of pages10
JournalNucleic acids research
Volume33
Issue number14
DOIs
Publication statusPublished - 2005
Externally publishedYes

ASJC Scopus subject areas

  • Genetics

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