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.
Mapping the Functional Domains of Yeast NMD3, the Nuclear Export Adapter for the 60 S Ribosomal Subunit*
J. Hedges,Y. Chen,Matthew West,C. Bussiere,Arlen W. Johnson
Published 2006 in Journal of Biological Chemistry
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- Publication year
2006
- Venue
Journal of Biological Chemistry
- Publication date
2006-12-01
- Fields of study
Biology, Medicine
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Semantic Scholar, PubMed
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