期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 19, 期 12, 页码 1316-+出版社
NATURE PORTFOLIO
DOI: 10.1038/nsmb.2403
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资金
- US National Center for Research Resources [5P41RR015301-10]
- US National Institute of General Medical Sciences from the US National Institutes of Health [8 P41 GM103403-10]
- US DOE [DE-AC02-06CH11357]
- Medical Faculty of the University of Heidelberg
- German Research Council [DFG Hu363/10-4]
- US National Institutes of Health National Cancer Institute grant [K22CA123152]
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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