The response regulator BvgA and RNA polymerase alpha subunit C-terminal domain bind simultaneously to different faces of the same segment of promoter DNA

Mol Cell. 2003 Jan;11(1):163-73. doi: 10.1016/s1097-2765(03)00007-8.


Examination of the binding of FeBABE-conjugated BvgA to the fha promoter of Bordetella pertussis has revealed that three dimers, formed by head-to-head association of monomers, bind one face of the DNA helix from the inverted-heptad primary binding site to the -35 region. The orientation of BvgA monomers within the dimers is the same as that recently demonstrated by X-ray crystallographic methods for a dimer of the C-terminal domain of NarL bound to DNA. Use of FeBABE conjugates of RNAP alpha subunit C-terminal domain showed that binding of this domain is linearly coincident with binding of the BvgA dimers, but to a different helical face. These results reveal a previously undescribed mode of interaction between RNAP alpha-CTD and a transcriptional activator.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Bordetella pertussis / genetics
  • Bordetella pertussis / metabolism
  • Cysteine / chemistry
  • Cysteine / metabolism
  • DNA / metabolism*
  • DNA-Directed RNA Polymerases / chemistry
  • DNA-Directed RNA Polymerases / genetics
  • DNA-Directed RNA Polymerases / metabolism*
  • Dimerization
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Promoter Regions, Genetic*
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protein Subunits / metabolism
  • Transcription Factors / chemistry
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*


  • Bacterial Proteins
  • BvgA protein, Bacteria
  • Protein Subunits
  • Transcription Factors
  • DNA
  • DNA-Directed RNA Polymerases
  • RNA polymerase alpha subunit
  • Cysteine