High impact information on NMD3

• The defect in Nmd3p recycling and the block in 60S export in both lsg1 and rpl10 mutants was also suppressed by mutant Nmd3 proteins that showed reduced binding to 60S subunits in vitro [1].
• When the 60S precursor particles are close to exit from the nucleus they associate with at least two export factors, Nmd3 and Mtr2 [2].
• Arx1 and Rei1 are found on late pre-60S ribosomal particles containing the export adaptor Nmd3 [3].
• A mutation in NMD3 was found to be lethal in the absence of XRN1, which encodes the major cytoplasmic exoribonuclease responsible for mRNA turnover [4].
• Molecular genetic analysis of NMD3 revealed that it is an essential gene required for stable 60S ribosomal subunits [4].

Biological context of NMD3

• Mapping the Functional Domains of Yeast NMD3, the Nuclear Export Adapter for the 60 S Ribosomal Subunit [5].
• The growth and mRNA decay defects of ts942 (grc5) cells were suppressed by overexpression of the NMD3 gene, encoding a protein shown to participate in a two-hybrid interaction with the nonsense-mediated decay protein Upf1p [6].
• GRC5 and NMD3 function in translational control of gene expression and interact genetically [7].

Anatomical context of NMD3

• Cells bearing a temperature-sensitive allele of NMD3 had decreased levels of 60S subunits at the nonpermissive temperature which resulted in the formation of half-mer polysomes [4].
• Here, we have carried out a mutational analysis of Nmd3 to better define the domains responsible for nucleocytoplasmic shuttling and ribosome binding [5].

Other interactions of NMD3

• These results suggest that in the absence of the ribosome, Nmd3 is not efficiently released from Crm1 at the NPC [8].

References