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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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Bibliographic Details
Main Authors: Ferreira-Cerca, Sébastien (Author) , Schäfer, Thorsten (Author) , Wesseling, Anne-Maria (Author) , Hurt, Ed (Author)
Format: Article (Journal)
Language:English
Published: 28 October 2012
In: Nature structural & molecular biology
Year: 2012, Volume: 19, Issue: 12, Pages: 1316-1323
ISSN:1545-9985
DOI:10.1038/nsmb.2403
Online Access:Verlag, Volltext: http://dx.doi.org/10.1038/nsmb.2403
Verlag, Volltext: https://www.nature.com/articles/nsmb.2403
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Author Notes: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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Summary: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.
Item Description:Gesehen am 21.09.2018
Physical Description:Online Resource
ISSN:1545-9985
DOI:10.1038/nsmb.2403

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