Unknown

Dataset Information

0

ATPase-dependent role of the atypical kinase Rio2 on the evolving pre-40S ribosomal subunit.


ABSTRACT: 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-Mg(2+) complex. The active site contains ADP-Mg(2+) and a phosphoaspartate intermediate typically found in Na(+), K(+) and Ca(2+) 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.

SUBMITTER: Ferreira-Cerca S 

PROVIDER: S-EPMC3515705 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

ATPase-dependent role of the atypical kinase Rio2 on the evolving pre-40S ribosomal subunit.

Ferreira-Cerca Sébastien S   Sagar Vatsala V   Schäfer Thorsten T   Diop Momar M   Wesseling Anne-Maria AM   Lu Haiyun H   Chai Eileen E   Hurt Ed E   LaRonde-LeBlanc Nicole N  

Nature structural & molecular biology 20121028 12


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-Mg(2+) complex. The active site contains ADP-Mg(2+) and a phosphoaspartate intermediate typically found in Na(+), K(+) and Ca(2+) ATPases but not protein kinases. Consistent with this finding, ctRio2 exhibits a robust ATPase activity in vitro. In vivo,  ...[more]

Similar Datasets

| S-EPMC5881545 | biostudies-literature
| S-EPMC5737503 | biostudies-literature
| S-EPMC5695908 | biostudies-literature
| S-EPMC2892368 | biostudies-literature
| S-EPMC3945201 | biostudies-literature
2024-07-27 | PXD054321 |
| S-EPMC3346313 | biostudies-literature
| S-EPMC2712965 | biostudies-literature
| S-EPMC4740875 | biostudies-literature
| S-EPMC4117770 | biostudies-literature