ArticleThe Journal of biological chemistry2013
Regulation of Deinococcus radiodurans RecA protein function via modulation of active and inactive nucleoprotein filament states.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- DNA damage response and cell cycle regulation in bacteria: a twist around the paradigm.Frontiers in microbiology · 2024Article
- Design and comparative characterization of RecA variants.Scientific reports · 2021Article
- DNA Damage Protection for Enhanced Bacterial Survival Under Simulated Low Earth Orbit Environmental Conditions inFrontiers in microbiology · 2021Article
- PprA Protein Inhibits DNA Strand Exchange and ATP Hydrolysis ofFrontiers in cell and developmental biology · 2021Article
- Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments ofInternational journal of molecular sciences · 2020Article
- Community Ecology of Deinococcus in Irradiated Soil.Microbial ecology · 2019Article
- Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species.FEMS microbiology reviews · 2019Review
- Bacillus subtilis RecA with DprA-SsbA antagonizes RecX function during natural transformation.Nucleic acids research · 2017Article
- The effects of pprI gene of Deinococcus radiodurans R1 on acute radiation injury of mice exposed to 60Co γ-ray radiation.Oncotarget · 2017Article
- Chromosomal transformation in Bacillus subtilis is a non-polar recombination reaction.Nucleic acids research · 2016Article
- A Decade of Biochemical and Structural Studies of the DNA Repair Machinery ofComputational and structural biotechnology journal · 2016Review
- Article
- Bacillus subtilis RecO and SsbA are crucial for RecA-mediated recombinational DNA repair.Nucleic acids research · 2015Article
- Recent progress in understanding the molecular mechanisms of radioresistance in Deinococcus bacteria.Extremophiles : life under extreme conditions · 2015Review
- Directed Evolution of RecA Variants with Enhanced Capacity for Conjugational Recombination.PLoS genetics · 2015Article
- Biochemical characterization of RecA variants that contribute to extreme resistance to ionizing radiation.DNA repair · 2015Article
- Functional roles of N-terminal and C-terminal domains in the overall activity of a novel single-stranded DNA binding protein of Deinococcus radiodurans.FEBS open bio · 2015Article
- Article
- Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic recombination.The Journal of biological chemistry · 2014Article
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Authors and funding
4 authors.
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Abstract
The RecA protein of Deinococcus radiodurans (DrRecA) has a central role in genome reconstitution after exposure to extreme levels of ionizing radiation. When bound to DNA, filaments of DrRecA protein exhibit active and inactive states that are readily interconverted in response to several sets of stimuli and conditions. At 30 °C, the optimal growth temperature, and at physiological pH 7.5, DrRecA protein binds to double-stranded DNA (dsDNA) and forms extended helical filaments in the presence of ATP. However, the ATP is not hydrolyzed. ATP hydrolysis of the DrRecA-dsDNA filament is activated by addition of single-stranded DNA, with or without the single-stranded DNA-binding protein. The ATPase function of DrRecA nucleoprotein filaments thus exists in an inactive default state under some conditions. ATPase activity is thus not a reliable indicator of DNA binding for all bacterial RecA proteins. Activation is effected by situations in which the DNA substrates needed to initiate recombinational DNA repair are present. The inactive state can also be activated by decreasing the pH (protonation of multiple ionizable groups is required) or by addition of volume exclusion agents. Single-stranded DNA-binding protein plays a much more central role in DNA pairing and strand exchange catalyzed by DrRecA than is the case for the cognate proteins in Escherichia coli. The data suggest a mechanism to enhance the efficiency of recombinational DNA repair in the context of severe genomic degradation in D. radiodurans.
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