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Structure of the four-way DNA junction and its interaction with proteins

Academic Article
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Overview

authors

  • Duckett, Derek
  • Murchie, A. I. H.
  • Giraudpanis, M. J. E.
  • Pohler, J. R.
  • Lilley, D. M. J.

publication date

  • January 1995

journal

  • Philosophical Transactions of the Royal Society of London Series B-Biological Sciences  Journal

abstract

  • The four-way DNA junction is an important intermediate in recombination processes; it is, the substrate for different enzyme activities. In solution, the junction adopts a right-handed, antiparallel-stacked X-structure formed by the pairwise coaxial-stacking of helical arms. The stereochemistry is determined by the juxtaposition of grooves and backbones, which is optimal when the smaller included angle is 60 degrees. The antiparallel structure has two distinct sides with major and minor groove-characteristics, respectively. The folding process requires the binding of metal cations, in the absence of which, the junction remains extended without helix-helix stacking. The geometry of the junction can be perturbed by the presence of certain base-base mispairs or phosphodiester discontinuities located at the point of strand exchange. The four-way DNA junction is selectively cleaved by a number of resolving enzymes. In a number of cases, these appear to recognize the minor groove face of the junction and are functionally divisible into activities that recognize and bind the junction, and a catalytic activity. Some possible mechanisms for the recognition of branched DNA structure are discussed.

subject areas

  • DNA
  • DNA-Binding Proteins
  • Nucleic Acid Conformation
  • Recombination, Genetic
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Identity

International Standard Serial Number (ISSN)

  • 0962-8436

Digital Object Identifier (DOI)

  • 10.1098/rstb.1995.0005

PubMed ID

  • 7746850
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Additional Document Info

start page

  • 27

end page

  • 36

volume

  • 347

issue

  • 1319

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