ArticleThe Journal of biological chemistry2016
Phosphorylation of Deinococcus radiodurans RecA Regulates Its Activity and May Contribute to Radioresistance.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 47 citations in OpenAlex.
- Rising from the fragments: a multi-factorial regulatory framework of DNA damage response in Deinococcus radiodurans.Extremophiles : life under extreme conditions · 2026Review
- The DR2416/DR2415 two-component system is responsible for the radioresistance of Deinococcus radiodurans.Antonie van Leeuwenhoek · 2025Article
- Adaptive laboratory evolution of Micrococcus luteus and identification of genes associated with radioresistance through genome-wide association study.Scientific reports · 2025Article
- Surviving the storm: exploring the role of natural transformation in nutrition and DNA repair of stressedApplied and environmental microbiology · 2025Article
- Application of the transposon-associated TnpB system of CRISPR-Cas in bacteria:Frontiers in microbiology · 2025Review
- Evolution and classification of Ser/Thr phosphatase PP2C family in bacteria: Sequence conservation, structures, domain distribution.PloS one · 2025Article
- Natural transformation-specific DprA coordinate DNA double-strand break repair pathways in heavily irradiatedApplied and environmental microbiology · 2024Article
- DNA damage response and cell cycle regulation in bacteria: a twist around the paradigm.Frontiers in microbiology · 2024Article
- New Insights into Radio-Resistance Mechanism Revealed by (Phospho)Proteome Analysis ofInternational journal of molecular sciences · 2023Article
- Complete genome sequence ofFrontiers in bioengineering and biotechnology · 2023Article
- Phosphorylation Regulation of a Histone-like HU Protein fromProtein and peptide letters · 2022Article
- Design and comparative characterization of RecA variants.Scientific reports · 2021Article
- PprA Protein Inhibits DNA Strand Exchange and ATP Hydrolysis ofFrontiers in cell and developmental biology · 2021Article
- Phosphoproteome Study ofFrontiers in microbiology · 2021Article
- Extremophilic Microorganisms for the Treatment of Toxic Pollutants in the Environment.Molecules (Basel, Switzerland) · 2020Review
- Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments ofInternational journal of molecular sciences · 2020Article
- LCN2 Is a Potential Biomarker for Radioresistance and Recurrence in Nasopharyngeal Carcinoma.Frontiers in oncology · 2020Article
- Construction, analysis and validation of co-expression network to understand stress adaptation in Deinococcus radiodurans R1.PloS one · 2020Article
- CLIC4 regulates radioresistance of nasopharyngeal carcinoma by iNOS after γ-rays but not carbon ions irradiation.American journal of cancer research · 2020Article
- Tyrosine Phosphorylation as a Widespread Regulatory Mechanism in Prokaryotes.Journal of bacteriology · 2019Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Deinococcus radiodurans has a remarkable capacity to survive exposure to extreme levels of radiation that cause hundreds of DNA double strand breaks (DSBs). DSB repair in this bacterium depends on its recombinase A protein (DrRecA). DrRecA plays a pivotal role in both extended synthesis-dependent strand annealing and slow crossover events of DSB repair during the organism's recovery from DNA damage. The mechanisms that control DrRecA activity during the D. radiodurans response to γ radiation exposure are unknown. Here, we show that DrRecA undergoes phosphorylation at Tyr-77 and Thr-318 by a DNA damage-responsive serine threonine/tyrosine protein kinase (RqkA). Phosphorylation modifies the activity of DrRecA in several ways, including increasing its affinity for dsDNA and its preference for dATP over ATP. Strand exchange reactions catalyzed by phosphorylated versus unphosphorylated DrRecA also differ. In silico analysis of DrRecA structure support the idea that phosphorylation can modulate crucial functions of this protein. Collectively, our findings suggest that phosphorylation of DrRecA enables the recombinase to selectively use abundant dsDNA substrate present during post-irradiation recovery for efficient DSB repair, thereby promoting the extraordinary radioresistance of D. radiodurans.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.