Rate and accuracy of bacterial protein synthesis revisited

Curr Opin Microbiol. 2008 Apr;11(2):141-7. doi: 10.1016/j.mib.2008.02.015. Epub 2008 Apr 8.


Our understanding of the accuracy of tRNA selection on the messenger RNA programmed ribosome has recently increased dramatically because of high-resolution crystal structures of the ribosome, cryo-electron microscopy reconstructions of its functional complexes, and fast kinetics experiments. Application of single-molecule spectroscopy with fluorescence resonance energy transfer to studies of tRNA selection by the ribosome has also provided new, albeit controversial, insights. Interestingly, when the fundamental trade-off between rate and accuracy in substrate-selective biosynthetic reactions is taken into account, some aspects of the current models of ribosome function appear strikingly suboptimal in the context of growing bacterial cells.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacteria / chemistry
  • Bacteria / genetics
  • Bacteria / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Kinetics
  • Protein Biosynthesis*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Transfer / genetics
  • RNA, Transfer / metabolism
  • Ribosomes / chemistry*
  • Ribosomes / metabolism
  • Spectrum Analysis / methods
  • Time Factors


  • Bacterial Proteins
  • RNA, Messenger
  • RNA, Transfer