Interaction of Escherichia coli RNA polymerase holoenzyme containing sigma 32 with heat shock promoters. DNase I footprinting and methylation protection

J Mol Biol. 1989 Dec 5;210(3):513-20. doi: 10.1016/0022-2836(89)90127-7.

Abstract

The DNase I protection pattern of E sigma 32 was assayed on three heat shock promoters, the E sigma 32 promoter for the groESL operon, P2 of the dnaKJ operon, and rpoD PHS, the E sigma 32 promoter upstream from rpoD. E sigma 32 protected each of these promoters from DNase I digestion from around -60 to around +20. Protection from dimethyl sulfate methylation was assayed at the groE promoter. E sigma 32 binding altered the sensitivity to methylation of bases in the vicinity of both the -10 and -35 regions. The DNase I footprints for the E sigma 32 promoters were very similar to the DNase I footprint of E sigma 70 on the lacUV5 promoter. After analyzing the DNase I footprints by taking into account the contacts predicted to be made by DNase I, it appeared that E sigma 32, like E sigma 70, contacts the DNA primarily on one face of the helix in the -35 region and on both faces in the -10 region.

Publication types

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

MeSH terms

  • Base Sequence
  • DNA-Binding Proteins / metabolism
  • DNA-Directed RNA Polymerases / metabolism*
  • Deoxyribonuclease I / pharmacology
  • Escherichia coli / genetics*
  • Gene Expression Regulation, Bacterial
  • Heat-Shock Proteins / genetics*
  • Methylation
  • Molecular Sequence Data
  • Promoter Regions, Genetic*
  • Sigma Factor / metabolism*
  • Transcription Factors / metabolism*

Substances

  • DNA-Binding Proteins
  • Heat-Shock Proteins
  • Sigma Factor
  • Transcription Factors
  • DNA-Directed RNA Polymerases
  • Deoxyribonuclease I