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J. Biol. Chem., Vol. 277, Issue 51, 49554-49561, December 20, 2002
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From the Max-Delbrück-Center for Molecular Medicine,
Robert-Rössle-Strasse 10, D-13092 Berlin, Germany and the
§ University of Cologne, Institute for Genetics,
Zülpicher Strasse 47, D-50674 Köln, Germany
Yeast SUMO (Smt3) and its mammalian
ortholog SUMO-1 are ubiquitin-like proteins that can reversibly be
conjugated to other proteins. Among the substrates for SUMO
modification in vertebrates are RanGAP1 and RanBP2/Nup358, two proteins
previously implicated in nucleocytoplasmic transport. Sumoylated
RanGAP1 binds to the nuclear pore complex via RanBP2/Nup358, a giant
nucleoporin, which was recently reported to act as a SUMO E3 ligase on
some nuclear substrates. However, no direct evidence for a role of the
SUMO system in nuclear transport has been obtained so far. By the use of conditional yeast mutants, we examined nuclear protein import in vivo. We show here that cNLS-dependent
protein import is impaired in mutants with defective Ulp1 and Uba2, two
enzymes involved in the SUMO conjugation reaction. In contrast, other
transport pathways such as rgNLS-mediated protein import and mRNA
export are not affected. Furthermore, we find that the yeast
importin-
A Lack of SUMO Conjugation Affects cNLS-dependent
Nuclear Protein Import in Yeast*
,
subunit Srp1 accumulates in the nucleus of
ulp1 and uba2 strains but not the importin-
subunit Kap95, indicating that a lack of Srp1 export might
impair cNLS import. In summary, our results provide evidence that SUMO
modification in yeast, as has been suspected for vertebrates, plays an
important role in nucleocytoplasmic trafficking.
*
This work was supported by a grant from the Deutsche
Forschungsgemeinschaft (DFG) (to K. S.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 49-30-9406-3736;
Fax: 49-30-9406-3363; E-mail: kstade@mdc-berlin.de.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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