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Key Intermediates in Ribosome Recycling Visualized by Time-Resolved Cryoelectron Microscopy.

Authors :
Fu Z
Kaledhonkar S
Borg A
Sun M
Chen B
Grassucci RA
Ehrenberg M
Frank J
Source :
Structure (London, England : 1993) [Structure] 2016 Dec 06; Vol. 24 (12), pp. 2092-2101. Date of Electronic Publication: 2016 Nov 03.
Publication Year :
2016

Abstract

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.<br /> (Copyright © 2016 Elsevier Ltd. All rights reserved.)

Details

Language :
English
ISSN :
1878-4186
Volume :
24
Issue :
12
Database :
MEDLINE
Journal :
Structure (London, England : 1993)
Publication Type :
Academic Journal
Accession number :
27818103
Full Text :
https://doi.org/10.1016/j.str.2016.09.014