The interaction of four-way DNA junctions with resolving enzymes
Copyright policy )The interaction of four-way DNA junctions with resolving enzymes
Four-way DNA (Holliday) junctions are resolved into duplex species by the action of the junction-resolving enzymes, nucleases selective for the structure of helical branchpoints. These have been isolated from bacteria and their phages, archaea, yeasts and mammals, including humans. They are all dimeric proteins that bind with high selectivity to DNA junctions and generate bilateral cleavage within the lifetime of the DNA–protein complex. Recent success in obtaining X-ray crystal structures of resolving enzymes bound to DNA junctions has revealed how the structural selectivity of these enzymes is achieved.
- University of Dundee United Kingdom
- Dow Chemical (United Kingdom) United Kingdom
Models, Molecular, 570, DNA repair, Substrate Specificity, T7 ENDONUCLEASE, MAMMALIAN-CELLS, Bacteriophage T7, T4 ENDONUCLEASE VII, Animals, Deoxyribonuclease I, Humans, CRYSTAL-STRUCTURE, YEAST, nuclease, REPAIR, genetic recombination, DNA, Cruciform, HOLLIDAY-JUNCTION, Base Sequence, GENE-3 ENDONUCLEASE, Holliday Junction Resolvases, RESOLUTION, Holiday junction, GENETIC-RECOMBINATION, Nucleic Acid Conformation, molecular recognition, Protein Binding
Models, Molecular, 570, DNA repair, Substrate Specificity, T7 ENDONUCLEASE, MAMMALIAN-CELLS, Bacteriophage T7, T4 ENDONUCLEASE VII, Animals, Deoxyribonuclease I, Humans, CRYSTAL-STRUCTURE, YEAST, nuclease, REPAIR, genetic recombination, DNA, Cruciform, HOLLIDAY-JUNCTION, Base Sequence, GENE-3 ENDONUCLEASE, Holliday Junction Resolvases, RESOLUTION, Holiday junction, GENETIC-RECOMBINATION, Nucleic Acid Conformation, molecular recognition, Protein Binding
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