The structural basis of Holliday junction resolution by T7 endonuclease I

Jonathan M. Hadden, Anne-Cécile Déclais, Stephen B. Carr, David M. J. Lilley and Simon E. V. Phillips ()
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Jonathan M. Hadden: Astbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds
Anne-Cécile Déclais: Cancer Research UK Nucleic Acid Structure Research Group, MSI/WTB complex, University of Dundee
Stephen B. Carr: Astbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds
David M. J. Lilley: Cancer Research UK Nucleic Acid Structure Research Group, MSI/WTB complex, University of Dundee
Simon E. V. Phillips: Astbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds

Nature, 2007, vol. 449, issue 7162, 621-624

Abstract: Holliday reading Genetic recombination between homologous DNA duplexes plays a critical role in the maintenance and propagation of genomes. The central intermediate of the process is the four-way (Holliday) junction that links two DNA duplexes. This is ultimately resolved to form two separate DNA duplexes. Junction resolvases of various types are found in prokaryotes, eukaryotes and their viruses. These nucleases are highly selective for the structure of the DNA branchpoint. Two groups now describe crystal structures of complexes of two different junction-resolving enzymes, endonuclease 1 (phage T7) and endonuclease VII (phage T4), each bound to DNA junctions. Both enzymes significantly distort the structure of the junction on binding. The new structures reveal how the enzymes are selective for DNA junctions, as well as the principles of the cleavage reaction.

Date: 2007
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DOI: 10.1038/nature06158

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