An archaeal Holliday junction resolving enzyme from Sulfolobus solfataricus exhibits unique properties

M Kvaratskhelia, Malcolm Frederick White

Research output: Other contribution

43 Citations (Scopus)

Abstract

The rearrangement and repair of DNA by homologous recombination often involves the creation of Holliday junctions, which must be cleaved by junction-specific endonucleases to yield recombinant duplex DNA products. Holliday junction resolving enzymes are a ubiquitous class of proteins with diverse structural and mechanistic characteristics. We have characterised an endonuclease (Hje) from the thermophilic crenarchaeote Sulfolobus solfataricus that exhibits a high degree of specificity for Holliday junctions via an apparently novel mechanism. Hje resolves four-way DNA junctions by the introduction of paired nicks in a reaction that is independent of the local nucleotide sequence, but is restricted solely to strands that are continuous in the stacked-X form of the junction. Three-way DNA junctions are cleaved only when the presence of a bulge in one strand allows the junction to stack in an analogous manner to four-way junctions. These properties differentiate Hje from all other known junction resolving enzymes. (C) 2000 Academic Press.

Original languageEnglish
Volume295
Publication statusPublished - 14 Jan 2000

Keywords

  • Holliday junction
  • archaea
  • endonuclease
  • resolving enzyme
  • homologous recombination
  • REPLICATION PROTEIN-A
  • DNA STRAND EXCHANGE
  • CRUCIFORM CUTTING ENDONUCLEASE
  • ESCHERICHIA-COLI
  • SACCHAROMYCES-CEREVISIAE
  • SCHIZOSACCHAROMYCES-POMBE
  • GENETIC-RECOMBINATION
  • RAD51 RECOMBINASE
  • CRYSTAL-STRUCTURE
  • RUVC RESOLVASE

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