Extent of duplex DNA underwinding induced by RecA protein binding in the presence of ATP. Academic Article uri icon

Overview

abstract

  • A method is described for the accurate determination of the superhelical density (omega) of highly underwound circular DNA molecules. Using this method, duplex DNA bound by RecA protein in the presence of ATP at pH 7.5 is found to be underwound by 39.6% (omega = -0.396), corresponding to a helical periodicity of 17.4 base-pairs per turn. The underwinding is increased to 41% (17.9 base-pairs per turn) in the presence of low levels of ATP gamma S, in good agreement with the 18.6 base-pairs per turn reported previously. In spite of the extensive underwinding, the distribution of DNA topoisomers produced by RecA protein binding is small. This indicates a high degree of structural uniformity among RecA-double-stranded DNA complexes in the presence of ATP.

publication date

  • February 5, 1989

Research

keywords

  • Adenosine Triphosphate
  • DNA Topoisomerases, Type I
  • DNA, Bacterial
  • Rec A Recombinases

Identity

Scopus Document Identifier

  • 0024511687

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(89)90219-2

PubMed ID

  • 2538631

Additional Document Info

volume

  • 205

issue

  • 3