The Integron Integrase Efficiently Prevents the Melting Effect of Escherichia coli Single-Stranded DNA-Binding Protein on Folded attC Sites
| Autor: | Céline Loot, David Bikard, Vincent Parissi, Jihane Amarir-Bouhram, Jose Antonio Escudero, Didier Mazel |
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| Přispěvatelé: | Plasticité du Génome Bactérien - Bacterial Genome Plasticity (PGB), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Microbiologie cellulaire et moléculaire et pathogénicité (MCMP), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), This work was supported by the Institut Pasteur, the Centre National de la Recherche Scientifique (CNRS-UMR3525), the European Union Seventh Framework Programme (FP7-HEALTH-2011-single-stage), and the Evolution and Transfer of Antibiotic Resistance (EvoTAR), European Project: 282004,EC:FP7:HEALTH,FP7-HEALTH-2011-single-stage,EVOTAR(2011), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Microbiologie Fondamentale et Pathogénicité (MFP) |
| Rok vydání: | 2014 |
| Předmět: |
DNA
Bacterial MESH: Integrases Plasma protein binding medicine.disease_cause Integron MESH: Attachment Sites Microbiological Microbiology DNA-binding protein Integrons 03 medical and health sciences chemistry.chemical_compound Escherichia coli medicine MESH: Protein Binding Molecular Biology Gene 030304 developmental biology Recombination Genetic Genetics 0303 health sciences Integrases biology MESH: Escherichia coli 030306 microbiology Escherichia coli Proteins Articles MESH: DNA Bacterial [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology MESH: Integrons Integrase DNA-Binding Proteins MESH: Nucleic Acid Conformation chemistry Attachment Sites Microbiological biology.protein Nucleic Acid Conformation MESH: Recombination Genetic MESH: DNA-Binding Proteins DNA Protein Binding |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2014, 196 (4), pp.762-771. ⟨10.1128/JB.01109-13⟩ Journal of Bacteriology, 2014, 196 (4), pp.762-771. ⟨10.1128/JB.01109-13⟩ |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | Integrons play a major role in the dissemination of antibiotic resistance genes among bacteria. Rearrangement of gene cassettes occurs by recombination between attI and attC sites, catalyzed by the integron integrase. Integron recombination uses an unconventional mechanism involving a folded single-stranded attC site. This site could be a target for several host factors and more precisely for proteins able to bind single-stranded DNA. One of these, Escherichia coli single-stranded DNA-binding protein (SSB), regulates many DNA processes. We studied the influence of this protein on integron recombination. Our results show the ability of SSB to strongly bind folded attC sites and to destabilize them. This effect was observed only in the absence of the integrase. Indeed, we provided evidence that the integrase is able to counterbalance the observed effect of SSB on attC site folding. We showed that IntI1 possesses an intrinsic property to capture attC sites at the moment of their extrusion, stabilizing them and recombining them efficiently. The stability of DNA secondary structures in the chromosome must be restrained to avoid genetic instability (mutations or deletions) and/or toxicity (replication arrest). SSB, which hampers attC site folding in the absence of the integrase, likely plays an important role in maintaining the integrity and thus the recombinogenic functionality of the integron attC sites. We also tested the RecA host factor and excluded any role of this protein in integron recombination. |
| Databáze: | OpenAIRE |
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