Cooperation between translating ribosomes and RNA polymerase in transcription elongation

Science. 2010 Apr 23;328(5977):504-8. doi: 10.1126/science.1184939.


During transcription of protein-coding genes, bacterial RNA polymerase (RNAP) is closely followed by a ribosome that translates the newly synthesized transcript. Our in vivo measurements show that the overall elongation rate of transcription is tightly controlled by the rate of translation. Acceleration and deceleration of a ribosome result in corresponding changes in the speed of RNAP. Moreover, we found an inverse correlation between the number of rare codons in a gene, which delay ribosome progression, and the rate of transcription. The stimulating effect of a ribosome on RNAP is achieved by preventing its spontaneous backtracking, which enhances the pace and also facilitates readthrough of roadblocks in vivo. Such a cooperative mechanism ensures that the transcriptional yield is always adjusted to translational needs at different genes and under various growth conditions.

Publication types

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

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Chloramphenicol / pharmacology
  • Codon
  • DNA-Directed RNA Polymerases / metabolism*
  • Escherichia coli / genetics*
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / biosynthesis
  • Escherichia coli Proteins / genetics*
  • Genes, Bacterial
  • Lac Operon
  • Peptide Chain Elongation, Translational / drug effects
  • Protein Biosynthesis* / drug effects
  • RNA, Bacterial / genetics
  • RNA, Bacterial / metabolism
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Ribosomes / metabolism*
  • Streptomycin / pharmacology
  • Transcription, Genetic* / drug effects
  • beta-Galactosidase / biosynthesis


  • Anti-Bacterial Agents
  • Codon
  • Escherichia coli Proteins
  • RNA, Bacterial
  • RNA, Messenger
  • Chloramphenicol
  • DNA-Directed RNA Polymerases
  • beta-Galactosidase
  • Streptomycin