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Molecular and Cellular Biology, July 2004, p. 6379-6392, Vol. 24, No. 14
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.14.6379-6392.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Fission Yeast Nup107-120 Complex Functionally Interacts with the Small GTPase Ran/Spi1 and Is Required for mRNA Export, Nuclear Pore Distribution, and Proper Cell Division

Siau Wei Baï,1 Jacques Rouquette,2,{dagger} Makoto Umeda,3,{dagger} Wolfgang Faigle,4 Damarys Loew,4 Shelley Sazer,3 and Valérie Doye1*

UMR 144 CNRS,1 Laboratoire de Spectrométrie de Masse Protéomique, Institut Curie, 75248 Paris Cedex 05,4 Laboratoire de Biologie Moléculaire Eucaryote (UMR 5099-CNRS), Université Paul Sabatier, 31062 Toulouse Cedex, France,2 Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 770303

Received 19 November 2003/ Returned for modification 26 January 2004/ Accepted 26 April 2004

We have characterized Schizosaccharomyces pombe open reading frames encoding potential orthologues of constituents of the evolutionarily conserved Saccharomyces cerevisiae Nup84 vertebrate Nup107-160 nuclear pore subcomplex, namely Nup133a, Nup133b, Nup120, Nup107, Nup85, and Seh1. In spite of rather weak sequence conservation, in vivo analyses demonstrated that these S. pombe proteins are localized at the nuclear envelope. Biochemical data confirmed the organization of these nucleoporins within conserved complexes. Although examination of the S. cerevisiae and S. pombe deletion mutants revealed different viability phenotypes, functional studies indicated that the involvement of this complex in nuclear pore distribution and mRNA export has been conserved between these highly divergent yeasts. Unexpectedly, microscopic analyses of some of the S. pombe mutants revealed cell division defects at the restrictive temperature (abnormal septa and mitotic spindles and chromosome missegregation) that were reminiscent of defects occurring in several S. pombe GTPase Ran (RanSp)/Spi1 cycle mutants. Furthermore, deletion of nup120 moderately altered the nuclear location of RanSp/Spi1, whereas overexpression of a nonfunctional RanSp/Spi1-GFP allele was specifically toxic in the {Delta}nup120 and {Delta}nup133b mutant strains, indicating a functional and genetic link between constituents of the S. pombe Nup107-120 complex and of the RanSp/Spi1 pathway.

* Corresponding author. Mailing address: UMR 144 CNRS-Institut Curie, 26 Rue d'Ulm, 75248 Paris Cedex 05, France. Phone: (33) 1 42 34 64 10. Fax: (33) 1 42 34 64 21. E-mail: vdoye{at}curie.fr.

{dagger} J.R. and M.U. contributed equally to this work.

Molecular and Cellular Biology, July 2004, p. 6379-6392, Vol. 24, No. 14
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.14.6379-6392.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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