A structural basis for allosteric control of DNA recombination by lambda integrase
| Autor: | Arthur Landy, Tapan K. Biswas, David J. Filman, Marta Radman-Livaja, Hideki Aihara, Tom Ellenberger |
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| Přispěvatelé: | Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM) |
| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Protein Conformation Molecular Nucleic Acid Conformation Pliability Protein Conformation Recombination Crystallography X-Ray Catalysis Article law.invention X-Ray DNA 03 medical and health sciences chemistry.chemical_compound Structure-Activity Relationship Allosteric Regulation Isomerism law Host chromosome Allosteric Regulation Attachment Sites [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Site-specific recombination Pliability 030304 developmental biology Genetics Recombination Genetic 0303 health sciences DNA Cruciform Multidisciplinary biology Base Sequence Integrases 030302 biochemistry & molecular biology Synapsis Cruciform/*chemistry/genetics/*metabolism Integrases/*chemistry/*metabolism Isomerism Models Microbiological/genetics Bacteriophage lambda/*enzymology Base Sequence Catalysis Crystallography Bacteriophage lambda Integrase chemistry Attachment Sites Microbiological Biophysics biology.protein Recombinant DNA Nucleic Acid Conformation Genetic/*genetics Structure-Activity Relationship Recombination In vitro recombination DNA |
| Zdroj: | Nature Nature, Nature Publishing Group, 2005, 435 (7045), pp.1059--66. ⟨10.1038/nature03657⟩ |
| ISSN: | 1476-4687 0028-0836 1476-4679 |
| DOI: | 10.1038/nature03657⟩ |
| Popis: | Site-specific DNA recombination is important for basic cellular functions including viral integration, control of gene expression, production of genetic diversity and segregation of newly replicated chromosomes, and is used by bacteriophage lambda to integrate or excise its genome into and out of the host chromosome. lambda recombination is carried out by the bacteriophage-encoded integrase protein (lambda-int) together with accessory DNA sites and associated bending proteins that allow regulation in response to cell physiology. Here we report the crystal structures of lambda-int in higher-order complexes with substrates and regulatory DNAs representing different intermediates along the reaction pathway. The structures show how the simultaneous binding of two separate domains of lambda-int to DNA facilitates synapsis and can specify the order of DNA strand cleavage and exchange. An intertwined layer of amino-terminal domains bound to accessory (arm) DNAs shapes the recombination complex in a way that suggests how arm binding shifts the reaction equilibrium in favour of recombinant products. |
| Databáze: | OpenAIRE |
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