ATPase-dependent role of the atypical kinase Rio2 on the evolving pre-40S ribosomal subunit
| Autor: | Haiyun Lu, Anne-Maria Wesseling, Ed Hurt, Sébastien Ferreira-Cerca, Thorsten Schäfer, Eileen Chai, Momar Diop, Vatsala Sagar, Nicole LaRonde-LeBlanc |
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| Rok vydání: | 2012 |
| Předmět: |
Adenosine Triphosphatases
Models Molecular 0303 health sciences biology Eukaryotic Large Ribosomal Subunit ATPase Protein subunit Protein Serine-Threonine Kinases Ribosome Article 03 medical and health sciences 0302 clinical medicine Biochemistry Structural Biology Eukaryotic initiation factor biology.protein Humans Eukaryotic Small Ribosomal Subunit Protein kinase A Eukaryotic Ribosome Molecular Biology Ribosomes 030217 neurology & neurosurgery 030304 developmental biology |
| Zdroj: | Nature structural & molecular biology |
| ISSN: | 1545-9985 |
| Popis: | Ribosome synthesis involves dynamic association of ribosome biogenesis factors with evolving pre-ribosomal particles. Rio2 is an atypical protein kinase required for pre-40S subunit maturation. We report the crystal structure of eukaryotic Rio2 with bound ATP/Mg2+. Unexpectedly, the structure reveals a phosphoaspartate intermediate with ADP/Mg2+ in the active site, typically found in Na+-, K+- and Ca2+-ATPases. 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. |
| Databáze: | OpenAIRE |
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