Bacterial translational control at atomic resolution

Trends Genet. 2003 Mar;19(3):155-61. doi: 10.1016/S0168-9525(03)00020-9.

Abstract

Translational regulation allows rapid adaptation of protein synthesis to environmental conditions. In prokaryotes, the synthesis of many RNA-binding proteins is regulated by a translational feedback mechanism involving a competition between their natural substrate and their binding site on mRNA, which are often thought to resemble each other. This article describes the case of threonyl-tRNA synthetase, which represses the translation of its own mRNA. Recent data provide the first opportunity to describe at the atomic level both the extent and the limit of mimicry between the way this enzyme recognizes tRNA(Thr) and its regulatory site in mRNA. The data also give some clues about how the binding of the synthetase to its mRNA inhibits translation.

Publication types

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

MeSH terms

  • Base Sequence
  • Conserved Sequence
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics*
  • Gene Expression Regulation, Bacterial*
  • Gene Expression Regulation, Enzymologic*
  • Genes, Bacterial
  • Models, Biological
  • Models, Molecular
  • Molecular Mimicry
  • Nucleic Acid Conformation
  • Operator Regions, Genetic
  • Protein Biosynthesis*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism*
  • RNA, Transfer, Thr / metabolism*
  • RNA-Binding Proteins / metabolism
  • Threonine-tRNA Ligase / chemistry
  • Threonine-tRNA Ligase / genetics*
  • Threonine-tRNA Ligase / metabolism

Substances

  • RNA, Messenger
  • RNA, Transfer, Thr
  • RNA-Binding Proteins
  • Threonine-tRNA Ligase