In vitro functional characterization of overproduced Escherichia coli katF/rpoS gene product

Biochemistry. 1993 Oct 19;32(41):11112-7. doi: 10.1021/bi00092a021.

Abstract

The katF/rpoS gene product (sigma s), a central regulator of stationary-phase gene expression in Escherichia coli, has been purified from an overproducing strain. sigma s was used as an immunogen for the production of monoclonal antibodies. Previous sequence analysis of sigma s strongly indicated homology to the sigma factor family. We show biochemically in this paper that sigma s is a sigma factor. This protein can bind to core RNA polymerase (E), and this binding can be competed effectively by the major E. coli transcription initiation factor, sigma 70. Immunopurified sigma s holoenzyme (E sigma s) transcribes the promoters of the bolAp1 gene and the xthA gene. Interestingly, both promoters can also be transcribed by sigma 70 holoenzyme (E sigma 70).

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • DNA-Directed RNA Polymerases / metabolism
  • Escherichia coli / genetics*
  • Gene Expression Regulation, Bacterial*
  • Molecular Sequence Data
  • Promoter Regions, Genetic
  • Sigma Factor / genetics*
  • Sigma Factor / metabolism
  • Transcription, Genetic

Substances

  • Bacterial Proteins
  • Sigma Factor
  • sigma factor KatF protein, Bacteria
  • DNA-Directed RNA Polymerases