Pregled bibliografske jedinice broj: 827792
The Walker A motif mutation recA4159 abolishes the SOS response and recombination in a recA730 mutant of Escherichia coli
The Walker A motif mutation recA4159 abolishes the SOS response and recombination in a recA730 mutant of Escherichia coli // Research in microbiology, 167 (2016), 6; 462-471 doi:10.1016/j.resmic.2016.04.005 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 827792 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
The Walker A motif mutation recA4159 abolishes the SOS response and recombination in a recA730 mutant of Escherichia coli
Autori
Šimatović, Ana ; Mitrikeski, Petar T. ; Vlašić, Ignacija ; Sopta, Mary ; Brčić-Kostić, Krunoslav
Izvornik
Research in microbiology (0923-2508) 167
(2016), 6;
462-471
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
RecA730 protein ; ATP binding ; Filament formation
Sažetak
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.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Ustanove:
Institut "Ruđer Bošković", Zagreb,
Institut za istraživanje i razvoj održivih eko sustava
Profili:
Marija-Mary Sopta
(autor)
Ana Šimatović
(autor)
Petar Mitrikeski
(autor)
Krunoslav Brčić-Kostić
(autor)
Ignacija Vlašić
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE