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Crystal structure of T4 endonuclease VII resolving a Holliday junction

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  • Christian Biertümpfel

    (National Institute of Diabetes and Digestive and Kidney Diseases, Laboratory of Molecular Biology, 9000 Rockville Pike, Bethesda, Maryland 20892, USA)

  • Wei Yang

    (National Institute of Diabetes and Digestive and Kidney Diseases, Laboratory of Molecular Biology, 9000 Rockville Pike, Bethesda, Maryland 20892, USA)

  • Dietrich Suck

    (European Molecular Biology Laboratory, Structural and Computational Biology Programme, Meyerhofstr. 1, 69117 Heidelberg, Germany)

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.

Suggested Citation

  • Christian Biertümpfel & Wei Yang & Dietrich Suck, 2007. "Crystal structure of T4 endonuclease VII resolving a Holliday junction," Nature, Nature, vol. 449(7162), pages 616-620, October.
    • Handle: RePEc:nat:nature:v:449:y:2007:i:7162:d:10.1038_nature06152
    DOI: 10.1038/nature06152
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    Cited by:

    1. Artur P. Kaczmarczyk & Anne-Cécile Déclais & Matthew D. Newton & Simon J. Boulton & David M. J. Lilley & David S. Rueda, 2022. "Search and processing of Holliday junctions within long DNA by junction-resolving enzymes," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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