title: Energetics of RecA-mediated recombination reactions. Without ATP hydrolysis RecA can mediate polar strand exchange but is unable to recycle.
abstract: We demonstrate that the step of DNA strand exchange during RecA-mediated recombination reaction can occur equally efficiently in the presence or absence of ATP hydrolysis. The polarity of strand exchange is the same when instead of ATP its non-hydrolyzable analog adenosine-5'-O-(3-thiotriphosphate) is used. We show that the ATP dependence of recombination reaction is limited to the post-exchange stages of the reactions. The low DNA affinity state of RecA protomers, induced after ATP hydrolysis, is necessary for the dissociation of RecA-DNA complexes at the end of the reaction. This dissociation of RecA from DNA is necessary for the release of recombinant DNA molecules from the complexes formed with RecA and for the recycling of RecA protomers for another round of the recombination reaction.
authors: Laboratoire d'Analyse Ultrastructurale, Université de Lausanne, Switzerland.
authors: W
authors: W
authors: Rosselli
authors: A
authors: A
authors: Stasiak
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism*; D010584:Bacteriophage phi X 174 / Q000235:genetics; D001483:Base Sequence; D004270:DNA, Circular / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D004279:DNA, Viral / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D008854:Microscopy, Electron; D008957:Models, Genetic; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D011485:Protein Binding; D011938:Rec A Recombinases / Q000378:metabolism* / Q000648:ultrastructure; D011995:Recombination, Genetic
chemical_list: D004270:DNA, Circular; D004279:DNA, Viral; D015345:Oligonucleotide Probes; C022571:adenosine 5'-O-(3-thiotriphosphate); D000255:Adenosine Triphosphate; D011938:Rec A Recombinases