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Published 10 December 2001. doi:10.1083/jcb.200108142
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© The Rockefeller University Press, 0021-9525/2001/12/923 $5.00
The Journal of Cell Biology, Volume 155, Number 6, December 10, 2001 923-936

Article

 Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex

Pierre-Emmanuel Gleizes1, Jacqueline Noaillac-Depeyre1, Isabelle Léger-Silvestre1, Frédéric Teulières1, Jean-Yves Dauxois2, Denys Pommet2, Marie-Claude Azum-Gelade1 and Nicole Gas1

1 Laboratoire de Biologie Moléculaire Eucaryote, Centre Nationale de la Recherche Scientifique and Université Paul Sabatier, 31062 Toulouse cedex, France
2 Ecole Nationale de la Statistique et de l'Analyse de l'Information, 35170 Bruz, France

Address correspondence to Pierre-Emmanuel Gleizes, Laboratoire de Biologie Moléculaire Eucaryote (CNRS - UMR 5099), 118 route de Narbonne, 31062 Toulouse cedex, France. Tel.: 33-561-33-59-26. Fax: 33-561-33-58-86. E-mail: gleizes{at}ibcg.biotoul.fr

To study the nuclear export of preribosomes, ribosomal RNAs were detected by in situ hybridization using fluorescence and EM, in the yeast Saccharomyces cerevisiae. In wild-type cells, semiquantitative analysis shows that the distributions of pre-40S and pre-60S particles in the nucleolus and the nucleoplasm are distinct, indicating uncoordinated transport of the two subunits within the nucleus. In cells defective for the activity of the GTPase Gsp1p/Ran, ribosomal precursors accumulate in the whole nucleus. This phenotype is reproduced with pre-60S particles in cells defective in pre-rRNA processing, whereas pre-40S particles only accumulate in the nucleolus, suggesting a tight control of the exit of the small subunit from the nucleolus. Examination of nucleoporin mutants reveals that preribosome nuclear export requires the Nup82p–Nup159p–Nsp1p complex. In contrast, mutations in the nucleoporins forming the Nup84p complex yield very mild or no nuclear accumulation of preribosome. Interestingly, domains of Nup159p required for mRNP trafficking are not necessary for preribosome export. Furthermore, the RNA helicase Dbp5p and the protein Gle1p, which interact with Nup159p and are involved in mRNP trafficking, are dispensable for ribosomal transport. Thus, the Nup82p–Nup159p–Nsp1p nucleoporin complex is part of the nuclear export pathways of preribosomes and mRNPs, but with distinct functions in these two processes.

Key Words: ribosome; nuclear export; nuclear pore complex; yeast; electron microscopy


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