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

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 i...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2009-09, Vol.106 (37), p.15702-15707
Main Authors: Fei, Jingyi, Bronson, Jonathan E, Hofman, Jake M, Srinivas, Rathi L, Wiggins, Chris H, Gonzalez, Ruben L. Jr
Format: Article
Language:English
Subjects:
Allosteric Regulation
Allosteric Site
Binding sites
Biological Sciences
Biophysical Phenomena
Conformity
Fluorescence Resonance Energy Transfer
Grants
Hybridity
Kinetics
Macromolecular Substances
Messenger RNA
Models, Molecular
Molecular structure
Peptide Elongation Factor G - chemistry
Peptide Elongation Factor G - metabolism
Peptide elongation factors
Protein Biosynthesis
Protein Conformation
Protein synthesis
Ribosomal proteins
Ribosomal Proteins - chemistry
Ribosomal Proteins - metabolism
Ribosomes
Ribosomes - chemistry
Ribosomes - metabolism
RNA, Transfer - chemistry
RNA, Transfer - genetics
RNA, Transfer - metabolism
Studies
Trajectories
Transfer RNA
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0908077106