Role of E.coli transcription-repair coupling factor Mfd in Nun-mediated transcription termination

J Mol Biol. 2003 Jun 13;329(4):655-62. doi: 10.1016/s0022-2836(03)00465-0.

Abstract

Phage HK022 Nun protein excludes phage lambda by binding nascent lambda-nut RNA and inducing termination and transcript release. In contrast, in a purified in vitro system, Nun arrests transcription on lambdaDNA templates without dissociation of the transcription elongation complex (TEC). Our evidence indicates that transcription-repair coupling factor (Mfd) frees Nun-arrested RNA polymerase. The activity of Nun is enhanced in an mfd-null mutant, consistent with prolonged association of Nun with the TEC. Furthermore, expression of lambda nut RNA in the mfd mutant titrates Nun, allowing superinfecting lambda to form plaques. Finally, addition of Mfd releases a Nun-arrested transcription complex in vitro.

MeSH terms

  • Bacterial Proteins / physiology*
  • Bacteriophage lambda / genetics
  • DNA Primers / chemistry
  • DNA-Directed RNA Polymerases / metabolism
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Galactokinase / genetics
  • Gene Expression Regulation, Viral
  • Homozygote
  • Lac Operon / physiology
  • Luciferases / metabolism
  • Models, Biological
  • Mutagenesis, Site-Directed
  • Plasmids
  • Polymerase Chain Reaction
  • RNA, Bacterial / genetics
  • Regulatory Sequences, Nucleic Acid
  • Streptavidin / chemistry
  • Terminator Regions, Genetic / genetics*
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Transcription Factors / physiology*
  • Transcription, Genetic*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*

Substances

  • Bacterial Proteins
  • DNA Primers
  • Nun protein, Enterobacteria phage HK022
  • RNA, Bacterial
  • Transcription Factors
  • Viral Proteins
  • transcription repair coupling factor protein, Bacteria
  • Streptavidin
  • Luciferases
  • Galactokinase
  • DNA-Directed RNA Polymerases