Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation
| Autor: | Rathi L. Srinivas, Jake M. Hofman, Jonathan E. Bronson, Ruben L. Gonzalez, Jingyi Fei, Chris H. Wiggins |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Ribosomal Proteins Quantitative Biology - Subcellular Processes Macromolecular Substances Protein Conformation Biophysics Biology Ribosome Biophysical Phenomena Allosteric Regulation RNA Transfer Ribosomal protein Large ribosomal subunit Protein biosynthesis Fluorescence Resonance Energy Transfer Peptide Elongation Factor G Subcellular Processes (q-bio.SC) Multidisciplinary Translation (biology) Biomolecules (q-bio.BM) Ribosomal RNA Biological Sciences Kinetics Biochemistry Quantitative Biology - Biomolecules Protein Biosynthesis FOS: Biological sciences Transfer RNA Ribosomes Allosteric Site |
| DOI: | 10.48550/arxiv.0909.0466 |
| Popis: | Determining the mechanism by which transfer RNAs (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 pre-translocation 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 towards 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 post-translocation 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. |
| Databáze: | OpenAIRE |
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