Ribosome Induces a Closed to Open Conformational Change in Release Factor 1
Krista Trappl,Simpson Joseph +1 more
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TL;DR: The results indicate that RF1 undergoes a large conformational change from a closed to an open form upon binding to the ribosome, consistent with the mechanism, in which high termination fidelity is achieved by linking stop codon recognition by RF1 to the change in conformation from closed to open state.
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About: This article is published in Journal of Molecular Biology. The article was published on 27 Mar 2016. and is currently open access. The article focuses on the topics: A-site & Ribosomal binding site.
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Citations
Translational termination without a stop codon
TL;DR: Structures reveal how ArfA rescues stalled ribosomes and suggest a general mechanism for release-factor–mediated translational termination in which a conformational switch leads to peptide release only when the appropriate signal is present in the A site.
82
Dynamic basis of fidelity and speed in translation: Coordinated multistep mechanisms of elongation and termination
TL;DR: This multidisciplinary approach has revealed the dynamic nature of translational control and uncovered how external cellular factors such as tRNA abundance and mRNA modifications affect the synthesis of the protein product.
38
Extensive ribosome and RF2 rearrangements during translation termination.
TL;DR: The authors' structures visualize how local rearrangements and spontaneous inter-subunit rotation poise the newly-made protein and RF2 to dissociate in preparation for ribosome recycling.
Conformational Control of Translation Termination on the 70S Ribosome.
TL;DR: The separation of codon recognition from the opening of the catalytic domain suggests how rearrangements in RF1 and in the ribosomal decoding center coordinate stop-codon recognition with peptide release, ensuring accurate translation termination.
30
Mechanism of Inhibition of Translation Termination by Blasticidin S.
TL;DR: The crystal structure of the potent termination inhibitor blasticidin S bound to the ribosomal 70S•release factor 1 (RF1) termination complex is reported, explaining the structural mechanism of inhibition.
21
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