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Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation

Fei, Jingyi; Bronson, Jonathan E.; Hofman, Jake M.; Stevens, Rathi L.; Wiggins, Chris H.; Gonzalez Jr., Ruben L.

Determining the mechanism by which tRNAs rapidly and precisely transit through the ribosomal A, P, and E sites during translation remains a major goal in the study of protein synthesis. Here, we report the real-time dynamics of the L1 stalk, a structural element of the large ribosomal subunit that is implicated in directing tRNA movements during translation. Within pretranslocation ribosomal complexes, the L1 stalk exists in a dynamic equilibrium between open and closed conformations. Binding of elongation factor G (EF-G) shifts this equilibrium toward the closed conformation through one of at least two distinct kinetic mechanisms, where the identity of the P-site tRNA dictates the kinetic route that is taken. Within posttranslocation complexes, L1 stalk dynamics are dependent on the presence and identity of the E-site tRNA. Collectively, our data demonstrate that EF-G and the L1 stalk allosterically collaborate to direct tRNA translocation from the P to the E sites, and suggest a model for the release of E-site tRNA.

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Title
Proceedings of the National Academy of Sciences
DOI
https://doi.org/10.1073/pnas.0908077106

More About This Work

Academic Units
Applied Physics and Applied Mathematics
Publisher
National Academy of Sciences
Published Here
September 20, 2014