title: Interaction of a four-way junction in DNA with T4 endonuclease VII.
abstract: The binding of a synthetic four-way junction in DNA by T4 endonuclease VII has been studied using gel retardation and footprint analysis. Two specific protein-DNA complexes have been observed, but only one is stable in the presence of moderate concentrations of salt. The footprint of T4 endonuclease VII in the salt-resistant complex has been probed using hydroxyl radicals generated by the reaction of iron(II)/EDTA with hydrogen peroxide. The hydroxyl radical cleavage pattern indicates protection of approximately 5 residues in two strands that are diametrically opposed across the junction point.
authors.affiliation: Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Hertfordshire, United Kingdom.
authors.forename: C A
authors.initials: CA
authors.lastname: Parsons
authors.forename: B
authors.initials: B
authors.lastname: Kemper
authors.forename: S C
authors.initials: SC
authors.lastname: West
mesh_terms: D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D004706:Endodeoxyribonucleases / Q000378:metabolism*; D005296:Ferrous Compounds; D006861:Hydrogen Peroxide; D006878:Hydroxides / Q000378:metabolism; D017665:Hydroxyl Radical; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009690:Nucleic Acid Conformation
chemical_list: D005296:Ferrous Compounds; D006878:Hydroxides; D046911:Macromolecular Substances; D017665:Hydroxyl Radical; D004247:DNA; D004492:Edetic Acid; D006861:Hydrogen Peroxide; D004706:Endodeoxyribonucleases; C035571:endodeoxyribonuclease VII