Recognition and selection of tRNA in translation

FEBS Lett. 2005 Feb 7;579(4):938-42. doi: 10.1016/j.febslet.2004.11.048.

Abstract

Aminoacyl-tRNA (aa-tRNA) is delivered to the ribosome in a ternary complex with elongation factor Tu (EF-Tu) and GTP. The stepwise movement of aa-tRNA from EF-Tu into the ribosomal A site entails a number of intermediates. The ribosome recognizes aa-tRNA through shape discrimination of the codon-anticodon duplex and regulates the rates of GTP hydrolysis by EF-Tu and aa-tRNA accommodation in the A site by an induced fit mechanism. Recent results of kinetic measurements, ribosome crystallography, single molecule FRET measurements, and cryo-electron microscopy suggest the mechanism of tRNA recognition and selection.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Crystallography
  • Protein Biosynthesis / physiology*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Transfer, Amino Acyl / metabolism*
  • Ribosomes / chemistry
  • Ribosomes / physiology

Substances

  • RNA, Messenger
  • RNA, Transfer, Amino Acyl