The Nug1 GTPase reveals an N-terminal RNA-binding domain that is essential for association with 60 S pre-ribosomal particles

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Abstract

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. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

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Bassler, J., Kallas, M., & Hurt, E. (2006). The Nug1 GTPase reveals an N-terminal RNA-binding domain that is essential for association with 60 S pre-ribosomal particles. Journal of Biological Chemistry, 281(34), 24737–24744. https://doi.org/10.1074/jbc.M604261200

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