Programmed drug-dependent ribosome stalling

Mol Microbiol. 2009 Feb;71(4):811-24. doi: 10.1111/j.1365-2958.2008.06576.x. Epub 2008 Nov 30.


The ribosome has the intrinsic capacity to monitor the sequence and structure of the nascent peptide. This fundamental property of the ribosome is often exploited in regulation of gene expression, in particular, for activation of expression of genes conferring resistance to ribosome-targeting antibiotics. Induction of expression of these genes is controlled by the programmed stalling of the ribosome at a regulatory open reading frame located upstream of the resistance cistron. Formation of the stalled translation complex depends on the presence of an antibiotic in the ribosome exit tunnel and the sequence of the nascent peptide. In this review, we summarize our current understanding of the molecular mechanisms of drug- and nascent peptide-dependent ribosome stalling.

Publication types

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

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / metabolism
  • Gene Expression Regulation, Bacterial*
  • Methyltransferases / metabolism
  • Nucleic Acid Conformation
  • Open Reading Frames
  • Protein Biosynthesis
  • RNA, Bacterial / metabolism
  • Ribosomes / drug effects*
  • Transcription Factors / metabolism


  • Anti-Bacterial Agents
  • Escherichia coli Proteins
  • RNA, Bacterial
  • SecM protein, E coli
  • Transcription Factors
  • Methyltransferases
  • rRNA (adenosine-O-2'-)methyltransferase