Ribosomal Translocation: One Step Closer to the Molecular Mechanism
- 27 January 2009
- journal article
- review article
- Published by American Chemical Society (ACS) in ACS Chemical Biology
- Vol. 4 (2) , 93-107
- https://doi.org/10.1021/cb8002946
Abstract
Protein synthesis occurs in ribosomes, the targets of numerous antibiotics. How these large and complex machines read and move along mRNA have proven to be challenging questions. In this Review, we focus on translocation, the last step of the elongation cycle in which movement of tRNA and mRNA is catalyzed by elongation factor G. Translocation entails large-scale movements of the tRNAs and conformational changes in the ribosome that require numerous tertiary contacts to be disrupted and reformed. We highlight recent progress toward elucidating the molecular basis of translocation and how various antibiotics influence tRNA−mRNA movement.Keywords
This publication has 130 references indexed in Scilit:
- Visualization of the Hybrid State of tRNA Binding Promoted by Spontaneous Ratcheting of the RibosomeMolecular Cell, 2008
- Spontaneous Intersubunit Rotation in Single RibosomesMolecular Cell, 2008
- Structures of modified eEF2·80S ribosome complexes reveal the role of GTP hydrolysis in translocationThe EMBO Journal, 2007
- Identification of Two Distinct Hybrid State Intermediates on the RibosomeMolecular Cell, 2007
- Kinetically Competent Intermediates in the Translocation Step of Protein SynthesisMolecular Cell, 2007
- Reverse Translocation of tRNA in the RibosomeMolecular Cell, 2006
- Structural basis for mRNA and tRNA positioning on the ribosomeProceedings of the National Academy of Sciences, 2006
- Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosomeProceedings of the National Academy of Sciences, 2006
- Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosomeNature, 1997
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991