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J. Biol. Chem., Vol. 283, Issue 12, 7877-7884, March 21, 2008

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Molecular Basis for the Recognition of Snurportin 1 by Importin β^*

From the Department of Biochemistry and Molecular Biology, State University of New York (SUNY) Upstate Medical University, Syracuse, New York 13210

The nuclear import of uridine-rich ribonucleoproteins is mediated by the transport adaptor snurportin 1 (SNP1). Similar to importin , SNP1 uses an N-terminal importin β binding (sIBB) domain to recruit the receptor importin β and gain access to the nucleus. In this study, we demonstrate that the sIBB domain has a bipartite nature, which contains two distinct binding determinants for importin β. The first determinant spans residues 25-65 and includes the previously identified importin IBB (IBB) region of homology. The second binding determinant encompasses residues 1-24 and resembles region 1011-1035 of the nucleoporin 153 (Nup153). The two binding determinants synergize within the sIBB domain to confer a low nanomolar binding affinity for importin β (K_d 2 nM) in an interaction that, in vitro, is displaced by RanGTP. We propose that in vivo the synergy of Nup153 and nuclear RanGTP promotes translocation of uridine-rich ribonucleoproteins into the nucleus.

Received for publication, November 6, 2007 , and in revised form, December 24, 2007.

The atomic coordinates and structure factors (code 2P8Q, 2Q5D) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by National Institutes of Health Grant GM074846. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains two supplemental figures.

¹ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750, E. Adams St., Syracuse, NY, 13210. Tel.: 315-464-8744; Fax: 315-464-8750; E-mail: cingolag{at}upstate.edu.

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