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Nucleic Acids Research 2005 33(14):4553-4562; doi:10.1093/nar/gki772
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Published online 12 August 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

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

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

Department of Bioresource Science and Technology, Graduate School of Biosphere Science, Hiroshima University Kagamiyama, Higashi-Hiroshima 739-8528, Japan

*To whom correspondence should be addressed. Tel: +81 82 424 7923; Fax: +81 82 424 7923; Email: kmizuta{at}hiroshima-u.ac.jp

Received May 26, 2005. Revised August 1, 2005. Accepted August 1, 2005.

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.


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