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Nucleic Acids Research 2005 33(18):5728-5739; doi:10.1093/nar/gki887
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Published online 12 October 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}oxfordjournals.org

Article

The essential WD-repeat protein Rsa4p is required for rRNA processing and intra-nuclear transport of 60S ribosomal subunits

Jesús de la Cruz*, Eloisa Sanz-Martínez1 and Miguel Remacha1

Departamento de Genética, Facultad de Biología, Universidad de Sevilla Avda Reina Mercedes, 6 Apartado 1095, E-41012 Sevilla, Spain 1Centro de Biología Molecular ‘Severo Ochoa’, CSIC and Universidad Autónoma de Madrid 28049-Cantoblanco, Madrid, Spain

*To whom correspondence should be addressed. Tel: +34 954 55 7106; Fax: +34 954 55 7104; Email: jdlcd{at}us.es

Received September 4, 2005. Revised September 20, 2005. Accepted September 20, 2005.

We report the characterization of a novel factor, Rsa4p (Ycr072cp), which is essential for the synthesis of 60S ribosomal subunits. Rsa4p is a conserved WD-repeat protein that seems to localize in the nucleolus. In vivo depletion of Rsa4p results in a deficit of 60S ribosomal subunits and the appearance of half-mer polysomes. Northern hybridization and primer extension analyses of pre-rRNA and mature rRNAs show that depletion of Rsa4p leads to the accumulation of the 27S, 25.5S and 7S pre-rRNAs, resulting in a reduction of the mature 25S and 5.8S rRNAs. Pulse–chase analyses of pre-rRNA processing reveal that, at least, this is due to a strong delay in the maturation of 27S pre-rRNA intermediates to mature 25S rRNA. Furthermore, depletion of Rsa4p inhibited the release of the pre-60S ribosomal particles from the nucleolus to the nucleoplasm, as judged by the predominantly nucleolar accumulation of the large subunit Rpl25-eGFP reporter construct. We propose that Rsa4p associates early with pre-60S ribosomal particles and provides a platform of interaction for correct processing of rRNA precursors and nucleolar release of 60S ribosomal subunits.

Correspondence may also be addressed to Miguel Remacha. Tel: +34 91 497 3001; Fax: +34 91 497 4799; Email: mremacha{at}cbm.uam.es


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A. Lebreton, J.-C. Rousselle, P. Lenormand, A. Namane, A. Jacquier, M. Fromont-Racine, and C. Saveanu
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[Abstract] [Full Text] [PDF]


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