Mapping the functional domains of yeast NMD3, the nuclear export adapter for the 60 S ribosomal subunit |
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Authors: | Hedges John Chen Yen-I West Matthew Bussiere Cyril Johnson Arlen W |
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Affiliation: | Section of Molecular Genetics and Microbiology and the Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78172-1095, USA. |
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Abstract: | 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. |
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