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. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Hedges, J., Chen, Y. I., West, M., Bussiere, C., & Johnson, A. W. (2006). Mapping the functional domains of yeast NMD3, the nuclear export adapter for the 60 S ribosomal subunit. Journal of Biological Chemistry, 281(48), 36579–36587. https://doi.org/10.1074/jbc.M606798200
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