ATPase-dependent role of the atypical kinase Rio2 on the evolving pre-40S ribosomal subunit
Ribosome synthesis involves dynamic association of ribosome-biogenesis factors with evolving preribosomal particles. Rio2 is an atypical protein kinase required for pre-40S subunit maturation. We report the crystal structure of eukaryotic Rio2-ATP-Mg2+ complex. The active site contains ADP-Mg2+ and...
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| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
28 October 2012
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| In: |
Nature structural & molecular biology
Year: 2012, Jahrgang: 19, Heft: 12, Pages: 1316-1323 |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb.2403 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1038/nsmb.2403 Verlag, Volltext: https://www.nature.com/articles/nsmb.2403 
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| Verfasserangaben: | Sébastien Ferreira-Cerca, Vatsala Sagar, Thorsten Schäfer, Momar Diop, Anne-Maria Wesseling, Haiyun Lu, Eileen Chai, Ed Hurt & Nicole LaRonde-LeBlanc |
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| 520 | |a Ribosome synthesis involves dynamic association of ribosome-biogenesis factors with evolving preribosomal particles. Rio2 is an atypical protein kinase required for pre-40S subunit maturation. We report the crystal structure of eukaryotic Rio2-ATP-Mg2+ complex. The active site contains ADP-Mg2+ and a phosphoaspartate intermediate typically found in Na+, K+ and Ca2+ ATPases but not protein kinases. Consistent with this finding, ctRio2 exhibits a robust ATPase activity in vitro. In vivo, Rio2 docks on the ribosome, with its active site occluded and its flexible loop positioned to interact with the pre-40S subunit. Moreover, Rio2 catalytic activity is required for its dissociation from the ribosome, a necessary step in pre-40S maturation. We propose that phosphoryl transfer from ATP to Asp257 in Rio2's active site and subsequent hydrolysis of the aspartylphosphate could be a trigger to power late cytoplasmic 40S subunit biogenesis. | ||
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