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Key Intermediates in Ribosome Recycling Visualized by Time-Resolved Cryoelectron Microscopy
Columbia Univ Coll Phys & Surg, Integrated Program Cellular Mol & Biomed Studies, 630 W 168th St, New York, NY 10032 USA..
Columbia Univ, Dept Biochem & Mol Biophys, 630 W 168th St, New York, NY 10027 USA..
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Biologiska sektionen, Institutionen för cell- och molekylärbiologi, Struktur- och molekylärbiologi.
Columbia Univ, Dept Biol Sci, New York, NY 10027 USA..
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2016 (engelsk)Inngår i: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 24, nr 12, s. 2092-2101Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Upon encountering a stop codon on mRNA, polypeptide synthesis on the ribosome is terminated by release factors, and the ribosome complex, still bound with mRNA and P-site-bound tRNA (post-termination complex, PostTC), is split into ribosomal subunits, ready for a new round of translational initiation. Separation of post-termination ribosomes into subunits, or "ribosome recycling,'' is promoted by the joint action of ribosome-recycling factor (RRF) and elongation factor G (EF-G) in a guanosine triphosphate (GTP) hydrolysis-dependent manner. Here we used a mixing-spraying-based method of time-resolved cryo-electron microscopy (cryo-EM) to visualize the short-lived intermediates of the recycling process. The two complexes that contain (1) both RRF and EF-G bound to the PostTC or (2) deacylated tRNA bound to the 30S subunit are of particular interest. Our observations of the native form of these complexes demonstrate the strong potential of time-resolved cryo-EM for visualizing previously unobservable transient structures.

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2016. Vol. 24, nr 12, s. 2092-2101
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URN: urn:nbn:se:uu:diva-316969DOI: 10.1016/j.str.2016.09.014ISI: 000393211300009PubMedID: 27818103OAI: oai:DiVA.org:uu-316969DiVA, id: diva2:1079450
Forskningsfinansiär
NIH (National Institute of Health), R01 GM55440 GM29169Swedish Research Council, 2015-04682Knut and Alice Wallenberg FoundationTilgjengelig fra: 2017-03-08 Laget: 2017-03-08 Sist oppdatert: 2018-01-13bibliografisk kontrollert

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