The NUG1 GTPase reveals and N-terminal RNA-binding domain that is essential for association with 60 S pre-ribosomal particles.

The putative yeast GTPase Nug1, which is associated with several pre-60 S particles in the nucleolus and nucleoplasm, consists of an N-terminal domain, which is found only in eukaryotic orthologues, and middle and C-terminal domains that are conserved throughout eukaryotes, bacteria, and archaea. Here, we analyzed the role of the ...
eukaryote-specific Nug1 N-domain (Nug1-N). We show that the essential Nug1-N is sufficient and necessary for nucle(ol)ar targeting and association with pre-60 S particles. Nug1-N exhibits RNA binding activity and is genetically linked in an allele-specific way to the pre-60 S factors Noc2, Noc3, and Dbp10. In contrast, the middle domain, which exhibits a circularly permuted GTPase fold and an intrinsic GTP hydrolysis activity in vitro, is not essential for cell growth. The conserved Nug1 C-domain, which has a yet uncharacterized fold, is also essential for ribosome biogenesis. Our findings suggest that Nug1 associates with pre-60 S subunits via its essential N-terminal RNA-binding domain and exerts a non-essential regulative role in pre-60 S subunit biogenesis via its central GTPase domain.
Mesh Terms:
Binding Sites, Carrier Proteins, DEAD-box RNA Helicases, Escherichia coli, GTP Phosphohydrolases, Nuclear Proteins, Nucleocytoplasmic Transport Proteins, Protein Binding, Protein Structure, Tertiary, RNA, RNA Helicases, RNA-Binding Proteins, Ribosomal Proteins, Ribosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
J. Biol. Chem.
Date: Aug. 25, 2006
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