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J. Biol. Chem., Vol. 275, Issue 37, 28575-28582, September 15, 2000
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From the The small GTPase Ran is essential for virtually
all nucleocytoplasmic transport events. It is hypothesized that Ran
drives vectorial transport of macromolecules into and out of the
nucleus via the establishment of a Ran gradient between the cytoplasm and nucleoplasm. Although Ran shuttles between the nucleus and cytoplasm, it is concentrated in the nucleus at steady state. We show
that nuclear transport factor 2 (NTF2) is required to concentrate Ran
in the nucleus in the budding yeast, Saccharomyces cerevisiae. To analyze the mechanism of Ran import into the
nucleus by NTF2, we use mutants in a variety of nuclear transport
factors along with biochemical analyses of NTF2 complexes. We find that Ran remains concentrated in the nucleus when importin-mediated protein
import is disrupted and demonstrate that NTF2 does not form a stable
complex with the transport receptor, importin-
The Mechanism of Ran Import into the Nucleus by Nuclear Transport
Factor 2*
§,
,
Department of Biochemistry, Emory University
School of Medicine and the ¶ Department of Biology, Emory
University, Atlanta, Georgia 30322
. Consistent with a
critical role for NTF2 in establishing and maintaining the Ran
gradient, we show that NTF2 is required for early embryogenesis in
Caenorhabditis elegans. Our data distinguish between two
possible mechanisms for Ran import by NTF2 and demonstrate that Ran
import is independent from importin--mediated protein import.
*
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.
Recipient of Biochemistry, Cell, and Molecular Biology
Predoctoral Training Grant 5T32GM08367.
**
Supported by U.S. Public Health Service Grant GMRO1GM40697 and
National Science Foundation Grant IBN-9631102.
Supported by National Institutes of Health Grant GM58728 and a
Biomedical Career Award from the Burroughs Wellcome Foundation. To whom
correspondence should be addressed: Dept. of Biochemistry, Emory
University, 1510 Clifton Rd., NE, Atlanta, GA 30322. Tel.: 404-727-4546; Fax: 404-727-3954; E-mail:
acorbe2@emory.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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