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J. Biol. Chem., Vol. 281, Issue 48, 36579-36587, December 1, 2006

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Mapping the Functional Domains of Yeast NMD3, the Nuclear Export Adapter for the 60 S Ribosomal Subunit^*

From the Section of Molecular Genetics and Microbiology and the Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78172-1095

Nuclear export of the large ribosomal subunit requires the adapter protein Nmd3p to provide a leucine-rich nuclear export signal that is recognized by the export receptor Crm1. Nmd3p binds to the pre-60 S subunit in the nucleus. After export to the cytoplasm, the release of Nmd3p depends on the ribosomal protein Rpl10p and the GTPase Lsg1p. Here, we have carried out a mutational analysis of Nmd3 to better define the domains responsible for nucleocytoplasmic shuttling and ribosome binding. We show that mutations in two regions of Nmd3p affect 60 S binding, suggesting that its binding to the subunit is multivalent.

Received for publication, July 17, 2006 , and in revised form, September 12, 2006.

^* This work was supported by National Institutes of Health Grant GM53655 (to A. W. J.). 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.

¹ Present address: Asuragen, 2150 Woodward St., Suite 100, Austin, TX 78744.

² Present address: Dept. of Cell Biology, University of Oklahoma Health Science Center, Oklahoma City, OK 73104.

³ To whom correspondence should be addressed: Section of Molecular Genetics and Microbiology, 1 University Station, A5000, University of Texas, Austin, TX 78712-1095. Tel.: 512-475-6350; Fax: 512-471-7088; E-mail: arlen{at}mail.utexas.edu.

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