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Characterization of the nuclear export adaptor protein Nmd3 in association with the 60S ribosomal subunit. (The Journal of Cell Biology 2010)
Authors: J Sengupta,C Bussiere,J Pallesen,M West,AW Johnson,J Frank
Three export receptors for the large (60S) ribosomal subunit have been identified in yeast, but Nmd3 is the only one of these that has a conserved role in vertebrates. This paper uses cryo-electron microscopy (cryo-EM) to map Nmd3 on the yeast 60S ribosomal subunit and demonstrates that Nmd3 maps interface to helices 38, 69 and 95 of 25S ribosomal RNA (rRNA), extending from the base of the rpL1 stalk to the base of the P-protein stalk at the ribosome subunit.
Biochemical studies presented here show that Nmd3 binds to the 60S ribosomal subunit but not to the 80S ribosome, supporting the dogma that the large and small ribosomal subunits exit separately from the nucleus. Helix 95 is adjacent to the binding site for rpL10 that is required for release of Nmd3 in the cytoplasm. Since rpL10 is part of the complex studied here, it is hypothesized that this complex is a late intermediate of 60S maturation. It is probable that the subsequent binding of Lsg1 and hydrolysis of its bound GTP induces a conformational change that results in the release of Nmd3.