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The cryo-EM structure of a ribosome-Ski2-Ski3-Ski8 helicase complex

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Kowalinski,  Eva
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Conti,  Elena
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Schmidt, C., Kowalinski, E., Shanmuganathan, V., Defenouillere, Q., Braunger, K., Heuer, A., et al. (2016). The cryo-EM structure of a ribosome-Ski2-Ski3-Ski8 helicase complex. Science, 354(6318), 1431-1433. doi:10.1126/science.aaf7520.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-57B6-4
Abstract
Ski2-Ski3-Ski8 (Ski) is a helicase complex functioning with the RNA-degrading exosome to mediate the 3-5' messenger RNA (mRNA) decay in turnover and quality-control pathways. We report that the Ski complex directly associates with 80S ribosomes presenting a short mRNA 3' overhang. We determined the structure of an endogenous ribosome-Ski complex using cryo electron microscopy (EM) with a local resolution of the Ski complex ranging from 4 angstroms (angstrom) in the core to about 10 angstrom for intrinsically flexible regions. Ribosome binding displaces the autoinhibitory domain of the Ski2 helicase, positioning it in an open conformation near the ribosomal mRNA entry tunnel. We observe that the mRNA 3 overhang is threaded directly from the small ribosomal subunit to the helicase channel of Ski2, primed for ongoing exosome-mediated 3'-5' degradation.