Interaction of a four-way junction in DNA with T4 endonuclease VII.
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.
Parsons
C A
CA
Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Hertfordshire, United Kingdom.
Kemper
B
B
West
S C
SC
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
D005296:Ferrous Compounds; D006878:Hydroxides; D046911:Macromolecular Substances; D017665:Hydroxyl Radical; D004247:DNA; D004492:Edetic Acid; D006861:Hydrogen Peroxide; D004706:Endodeoxyribonucleases; C035571:endodeoxyribonuclease VII