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J. Biol. Chem., Vol. 276, Issue 48, 45349-45357, November 30, 2001
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From the Department of Oncological Sciences, Huntsman Cancer
Institute, University of Utah, Salt Lake City, Utah 84112
Traffic between the nucleus and cytoplasm takes
place through a macromolecular structure termed the nuclear pore
complex. To understand how the vital process of nucleocytoplasmic
transport occurs, the contribution of individual pore proteins must be
elucidated. One such protein, the nucleoporin Nup153, is localized to
the nuclear basket of the pore complex and has been shown to be a central component of the nuclear transport machinery. Perturbation of
Nup153 function was demonstrated previously to block the export of
several classes of RNA cargo. Moreover, these studies also showed that
Nup153 can stably associate with RNA in vitro. In this
study, we have mapped a domain within Nup153, encompassing amino acids
250-400 in human Nup153, that is responsible for RNA association.
After cloning this region of Xenopus Nup153, we performed a
cross-species analysis. Despite variation in sequence conservation between Drosophila, Xenopus, and human, this
domain of Nup153 displayed robust RNA binding activity in each case,
indicating that this property is a hallmark feature of Nup153 and
pointing toward a subset of amino acid residues that are key to
conferring this ability. We have further determined that a recombinant
fragment of Nup153 can bind directly to RNA and that this fragment can interact with endogenous RNA targets. Our findings identify a functionally conserved domain in Nup153 and suggest a role for RNA
binding in Nup153 function at the nuclear pore.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF434196
RNA Association Defines a Functionally Conserved Domain in the
Nuclear Pore Protein Nup153*
*
This work was supported by National Institutes of Health
Grant GM61275, a Burroughs Wellcome Career Award in Biomedical Science, and the Huntsman Cancer Foundation.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: Dept. of Oncological
Sciences, Huntsman Cancer Institute, University of Utah, 2000 Circle of
Hope, Salt Lake City, UT 84112. Tel.: 801-585-7123; Fax: 801-585-0900;
E-mail: katharine.ullman@hci.utah.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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