The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy

Ziao Fu, Gabriele Indrisiunaite, Sandip Kaledhonkar, Binita Shah, Ming Sun, Bo Chen, Robert A. Grassucci, Måns Ehrenberg and Joachim Frank ()
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Ziao Fu: Columbia University
Gabriele Indrisiunaite: Uppsala University
Sandip Kaledhonkar: Columbia University
Binita Shah: Barnard College
Ming Sun: Columbia University
Bo Chen: Columbia University
Robert A. Grassucci: Columbia University
Måns Ehrenberg: Uppsala University
Joachim Frank: Columbia University

Nature Communications, 2019, vol. 10, issue 1, 1-7

Abstract: Abstract When the ribosome encounters a stop codon, it recruits a release factor (RF) to hydrolyze the ester bond between the peptide chain and tRNA. RFs have structural motifs that recognize stop codons in the decoding center and a GGQ motif for induction of hydrolysis in the peptidyl transfer center 70 Å away. Surprisingly, free RF2 is compact, with only 20 Å between its codon-reading and GGQ motifs. Cryo-EM showed that ribosome-bound RFs have extended structures, suggesting that RFs are compact when entering the ribosome and then extend their structures upon stop codon recognition. Here we use time-resolved cryo-EM to visualize transient compact forms of RF1 and RF2 at 3.5 and 4 Å resolution, respectively, in the codon-recognizing ribosome complex on the native pathway. About 25% of complexes have RFs in the compact state at 24 ms reaction time, and within 60 ms virtually all ribosome-bound RFs are transformed to their extended forms.

Date: 2019
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DOI: 10.1038/s41467-019-10608-z

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