Development of RNA polymerase-promoter contacts during open complex formation

J Mol Biol. 1991 Aug 5;220(3):585-97. doi: 10.1016/0022-2836(91)90102-c.

Abstract

We have charted the movements of E sigma 32 RNA polymerase at the heat-shock promoter PgroE throughout open complex formation, using hydroxyl radical footprinting. In combination with methylation protection and DNase I experiments, these data suggest the following model for open complex formation. E sigma 32 initially anchors itself in the upstream region of the promoter forming the first closed complex, RPC1; in this complex the enzyme makes backbone contacts in the -35 region of the promoter that are maintained throughout open complex formation. An isomerization follows resulting in a second closed complex, RPC2; in this complex the enzyme makes base-specific and backbone contacts in the -10 region that are almost identical to those found in the open complex. Thus, at the groE promoter, upstream contacts are established in RPC1 and downstream contacts in RPC2. A similar pattern of backbone contacts was obtained for E sigma 32 bound in the open complex at two additional heat-shock promoters, suggesting that the overall topology of holoenzyme in the open complex is similar regardless of sequence variations in the promoter.

Publication types

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

MeSH terms

  • Base Sequence
  • Binding Sites
  • DNA, Bacterial / genetics
  • DNA, Bacterial / isolation & purification
  • DNA-Directed RNA Polymerases / metabolism*
  • Deoxyribonuclease I
  • Escherichia coli / enzymology
  • Escherichia coli / genetics*
  • Free Radicals
  • Hydroxides
  • Hydroxyl Radical
  • Methylation
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Promoter Regions, Genetic*
  • Restriction Mapping

Substances

  • DNA, Bacterial
  • Free Radicals
  • Hydroxides
  • Hydroxyl Radical
  • DNA-Directed RNA Polymerases
  • Deoxyribonuclease I