The K+-dependent GTPase Nug1 is implicated in the association of the helicase Dbp10 to the immature peptidyl transferase centre during ribosome maturation

Nucleic Acids Research
Rizos-Georgios ManikasEd Hurt

Abstract

Ribosome synthesis employs a number of energy-consuming enzymes in both eukaryotes and prokaryotes. One such enzyme is the conserved circularly permuted GTPase Nug1 (nucleostemin in human). Nug1 is essential for 60S subunit assembly and nuclear export, but its role and time of action during maturation remained unclear. Based on in vitro enzymatic assays using the Chaetomium thermophilum (Ct) orthologue, we show that Nug1 exhibits a low intrinsic GTPase activity that is stimulated by potassium ions, rendering Nug1 a cation-dependent GTPase. In vivo we observe 60S biogenesis defects upon depletion of yeast Nug1 or expression of a Nug1 nucleotide-binding mutant. Most prominently, the RNA helicase Dbp10 was lost from early pre-60S particles, which suggested a physical interaction that could be reconstituted in vitro using CtNug1 and CtDbp10. In vivo rRNA-protein crosslinking revealed that Nug1 and Dbp10 bind at proximal and partially overlapping sites on the 60S pre-ribosome, most prominently to H89 that will constitute part of the peptidyl transferase center (PTC). The binding sites of Dbp10 are the same as those identified for the prokaryotic helicase DbpA bound to the 50S subunit. We suggest that Dbp10 and DbpA are performing a ...Continue Reading

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Citations

Jan 3, 2018·Nucleic Acids Research·Gertrude ZisserHelmut Bergler
Nov 24, 2018·Nature Reviews. Molecular Cell Biology·Sebastian Klinge, John L Woolford
Oct 30, 2019·Journal of Molecular Evolution·Antoine Danchin, Pablo Iván Nikel
Jan 8, 2017·The Biochemical Journal·Salini Konikkat, John L Woolford
May 23, 2018·Nucleic Acids Research·Francisco Espinar-MarchenaJesús de la Cruz
Apr 25, 2018·The Journal of Cell Biology·Stephanie BiedkaJohn L Woolford
Dec 20, 2018·Annual Review of Biochemistry·Jochen Baßler, Ed Hurt
Aug 29, 2021·Proceedings of the National Academy of Sciences of the United States of America·Jan Philip WurmRemco Sprangers

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