Ribosomal translocation: one step closer to the molecular mechanism

ACS Chem Biol. 2009 Feb 20;4(2):93-107. doi: 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.

Publication types

  • Review

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Models, Molecular*
  • Models, Structural
  • Molecular Conformation*
  • Peptide Chain Elongation, Translational / drug effects
  • Peptide Chain Elongation, Translational / physiology*
  • Peptide Elongation Factor G* / chemistry
  • Peptide Elongation Factor G* / metabolism
  • Protein Synthesis Inhibitors / pharmacology
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Transfer / genetics
  • RNA, Transfer / metabolism
  • Ribosomes* / chemistry
  • Ribosomes* / metabolism

Substances

  • Anti-Bacterial Agents
  • Peptide Elongation Factor G
  • Protein Synthesis Inhibitors
  • RNA, Messenger
  • RNA, Transfer