The Walker A motif mutation recA4159 abolishes the SOS response and recombination in a recA730 mutant of Escherichia coli
| Autor: | Krunoslav Brčić-Kostić, Petar T. Mitrikeski, Mary Sopta, Ana Šimatović, Ignacija Vlašić |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
DNA Repair DNA repair Mutant Biology Microbiology 03 medical and health sciences SOS Response (Genetics) chemistry.chemical_compound Adenosine Triphosphate ATP hydrolysis Escherichia coli SOS response SOS Response Genetics Molecular Biology Recombination Genetic RecA730 protein ATP binding Filament formation Walker motifs Wild type General Medicine Cell biology Rec A Recombinases 030104 developmental biology chemistry Biochemistry Mutant Proteins Protein Multimerization Adenosine triphosphate Protein Binding |
| Popis: | In bacteria, the RecA protein forms recombinogenic filaments required for the SOS response and DNA recombination. In order to form a recombinogenic filament, wild type RecA needs to bind ATP and to interact with mediator proteins. The RecA730 protein is a mutant version of RecA with superior catalytic abilities, allowing filament formation without the help of mediator proteins. The mechanism of RecA730 filament formation is not well understood, and the question remains as to whether the RecA730 protein requires ATP binding in order to become competent for filament formation. We examined two mutants, recA730, 4159 (presumed to be defective for ATP binding) and recA730, 2201 (defective for ATP hydrolysis), and show that they have different properties with respect to SOS induction, conjugational recombination and double-strand break repair. We show that ATP binding is essential for all RecA730 functions, while ATP hydrolysis is required only for double-strand break repair. Our results emphasize the similarity of the SOS response and conjugational recombination, neither of which requires ATP hydrolysis by RecA730. |
| Databáze: | OpenAIRE |
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