Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 9, Pages 1043-U106Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2098
Keywords
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Funding
- Burroughs Wellcome Fund [CABS 1004856]
- US National Science Foundation [MCB 0644262]
- US National Institute of General Medical Sciences [GM 084288]
- Columbia University
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Translocation of tRNAs through the ribosome during protein synthesis involves large-scale structural rearrangement of the ribosome and ribosome-bound tRNAs that is accompanied by extensive and dynamic remodeling of tRNA-ribosome interactions. How the rearrangement of individual tRNA-ribosome interactions influences tRNA movement during translocation, however, remains largely unknown. To address this question, we used single-molecule FRET to characterize the dynamics of ribosomal pretranslocation (PRE) complex analogs carrying either wild-type or systematically mutagenized tRNAs. Our data reveal how specific tRNA-ribosome interactions regulate the rate of PRE complex rearrangement into a critical, on-pathway translocation intermediate and how these interactions control the stability of the resulting configuration. Notably, our results suggest that the conformational flexibility of the tRNA molecule has a crucial role in directing the structural dynamics of the PRE complex during translocation.
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