Core RNA polymerase from E. coli induces a major change in the domain arrangement of the sigma 70 subunit

Mol Cell. 1999 Feb;3(2):229-38. doi: 10.1016/s1097-2765(00)80313-5.

Abstract

Luminescence resonance energy transfer measurements were used to show that binding of E. coli core RNA polymerase induced major changes in interdomain distances in the sigma 70 subunit. The simplest model describing core-induced changes in sigma 70 involves a movement of the conserved region 1 by approximately 20 A and the conserved region 4.2 by approximately 15 A with respect to conserved region 2. The core-induced movement of region 1 (autoinhibition domain) and region 4.2 (DNA-binding domain) provides structural rationale for allosteric regulation of sigma 70 DNA binding properties by the core and suggests that this regulation may not only involve directly the autoinhibition domain of sigma 70 but also could involve a modulation of spacing between DNA-binding domains of sigma 70 induced by binding of core RNAP.

Publication types

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

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Coumarins
  • DNA-Directed RNA Polymerases / chemistry*
  • DNA-Directed RNA Polymerases / genetics
  • DNA-Directed RNA Polymerases / metabolism
  • Energy Transfer
  • Escherichia coli / enzymology*
  • Fluorescent Dyes
  • Maleimides
  • Mutagenesis, Site-Directed
  • Pentetic Acid
  • Protein Binding
  • Protein Conformation*
  • Sigma Factor / chemistry*
  • Sigma Factor / genetics
  • Sigma Factor / metabolism
  • Spectrometry, Fluorescence

Substances

  • Bacterial Proteins
  • Coumarins
  • Fluorescent Dyes
  • Maleimides
  • Sigma Factor
  • maleimide
  • Pentetic Acid
  • RNA polymerase sigma 70
  • DNA-Directed RNA Polymerases
  • 7-amino-4-methylcoumarin-3-acetic acid