Hedges John, Chen Yen-I, West Matthew, Bussiere Cyril, Johnson Arlen W
Section of Molecular Genetics and Microbiology and the Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78172-1095, USA.
J Biol Chem. 2006 Dec 1;281(48):36579-87. doi: 10.1074/jbc.M606798200. Epub 2006 Oct 2.
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.
大核糖体亚基的核输出需要衔接蛋白Nmd3p提供一个富含亮氨酸的核输出信号,该信号可被输出受体Crm1识别。Nmd3p在细胞核中与前60 S亚基结合。输出到细胞质后,Nmd3p的释放依赖于核糖体蛋白Rpl10p和GTP酶Lsg1p。在此,我们对Nmd3进行了突变分析,以更好地确定负责核质穿梭和核糖体结合的结构域。我们发现,Nmd3p两个区域的突变会影响60 S的结合,这表明它与亚基的结合是多价的。