Activation of prokaryotic transcription through arbitrary protein-protein contacts

Nature. 1997 Apr 10;386(6625):627-30. doi: 10.1038/386627a0.


Many transcriptional activators in prokaryotes are known to bind near a promoter and contact RNA polymerase, but it is not clear whether a protein-protein contact between an activator and RNA polymerase is enough to activate gene transcription. Here we show that contact between a DNA-bound protein and a heterologous protein domain fused to RNA polymerase can elicit transcriptional activation; moreover, the strength of this engineered protein-protein interaction determines the amount of gene activation. Our results indicate that an arbitrary interaction between a DNA-bound protein and RNA polymerase can activate transcription. We also find that when the DNA-bound 'activator' makes contact with two different components of the polymerase, the effect of these two interactions on transcription is synergistic.

Publication types

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

MeSH terms

  • Bacteriophage lambda / genetics
  • Binding Sites
  • Cloning, Molecular
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • DNA-Directed RNA Polymerases / metabolism*
  • Escherichia coli / genetics
  • Mutation
  • Plasmids
  • Prokaryotic Cells
  • Protein Binding
  • Recombinant Fusion Proteins / metabolism
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism
  • Transcriptional Activation*
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins


  • DNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins
  • phage repressor proteins
  • DNA-Directed RNA Polymerases