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Elife. 2013 Jun 4;2:e00411. doi: 10.7554/eLife.00411.

Cryo-EM visualization of the ribosome in termination complex with apo-RF3 and RF1.

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  • 1Department of Biochemistry and Molecular Biophysics , Howard Hughes Medical Institute, Columbia University , New York City , United States.


Termination of messenger RNA translation in Bacteria and Archaea is initiated by release factors (RFs) 1 or 2 recognizing a stop codon in the ribosomal A site and releasing the peptide from the P-site transfer RNA. After release, RF-dissociation is facilitated by the G-protein RF3. Structures of ribosomal complexes with RF1 or RF2 alone or with RF3 alone-RF3 bound to a non-hydrolyzable GTP-analog-have been reported. Here, we present the cryo-EM structure of a post-termination ribosome containing both apo-RF3 and RF1. The conformation of RF3 is distinct from those of free RF3•GDP and ribosome-bound RF3•GDP(C/N)P. Furthermore, the conformation of RF1 differs from those observed in RF3-lacking ribosomal complexes. Our study provides structural keys to the mechanism of guanine nucleotide exchange on RF3 and to an L12-mediated ribosomal recruitment of RF3. In conjunction with previous observations, our data provide the foundation to structurally characterize the complete action cycle of the G-protein RF3. DOI:http://dx.doi.org/10.7554/eLife.00411.001.


Cryo-EM; E. coli; L7/L12; RF1; RF3; Ribosome; Structure

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