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Nucleic Acids Research Advance Access published online on September 27, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn625
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Nuclear export competence of pre-40S subunits in fission yeast requires the ribosomal protein Rps2

Audrey Perreault, Clément Bellemer and Francois Bachand*

RNA Group, Department of Biochemistry, Université de Sherbrooke, Québec, Canada

*To whom correspondence should be addressed. Tel: +819 820 6868; Fax: +819 564 5340; Email: f.bachand{at}usherbrooke.ca Present address: Clément Bellemer, Laboratoire de Biologie Moléculaire Eucaryote, CNRS and Université Paul Sabatier, Toulouse, France

Received April 29, 2008. Revised September 9, 2008. Accepted September 12, 2008.

Ribosome biogenesis is an evolutionarily conserved pathway that requires ribosomal and nonribosomal proteins. Here, we investigated the role of the ribosomal protein S2 (Rps2) in fission yeast ribosome synthesis. As for many budding yeast ribosomal proteins, Rps2 was essential for cell viability in fission yeast and the genetic depletion of Rps2 caused a complete inhibition of 40S ribosomal subunit production. The pattern of pre-rRNA processing upon depletion of Rps2 revealed a reduction of 27SA2 pre-rRNAs and the concomitant production of 21S rRNA precursors, consistent with a role for Rps2 in efficient cleavage at site A2 within the 32S pre-rRNA. Importantly, kinetics of pre-rRNA accumulation as determined by rRNA pulse-chases assays indicated that a small fraction of 35S precursors matured into 20S-containing particles, suggesting that most 40S precursors were rapidly degraded in the absence of Rps2. Analysis of steady-state RNA levels revealed that some pre-40S particles were produced in Rps2-depleted cells, but that these precursors were retained in the nucleolus. Our findings suggest a role for Rps2 in a mechanism that monitors pre-40S export competence.


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[Abstract] [Full Text] [PDF]


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