Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 37, Pages 15702-15707Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0908077106
Keywords
dynamics; single-molecule FRET; ribosome; translocation
Categories
Funding
- Burroughs Wellcome Fund [CABS 1004856]
- National Science Foundation (NSF) [MCB 0644262]
- National Institutes of Health (NIH)-National Institute of General Medical Sciences [1RO1GM084288-01, 1U54CA121852-01A1, 5PN2EY016586-03]
- NSF Research Experience for Undergraduates
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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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