ArticleThe Journal of biological chemistry2009
Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 83 citations in OpenAlex.
- Structural and biochemical characterization of a novel DinG containing an endonuclease domain.Cellular and molecular life sciences : CMLS · 2026Article
- The DinG exonuclease acts as a primary quality controller to remove unprocessed ribosomal RNAs.Nucleic acids research · 2026Article
- Article
- Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025Review
- Coordination of cell division and chromosome segregation by iron and a sRNA inFrontiers in microbiology · 2024Article
- Exploring the G-quadruplex binding and unwinding activity of the bacterial FeS helicase DinG.Scientific reports · 2023Article
- Identification of a Novel Chromate and Selenite Reductase FesR inFrontiers in microbiology · 2022Article
- Alternative complexes formed by the Escherichia coli clamp loader accessory protein HolC (x) with replication protein HolD (ψ) and repair protein YoaA.DNA repair · 2021Article
- Positioning Diverse Type IV Structures and Functions Within Class 1 CRISPR-Cas Systems.Frontiers in microbiology · 2021Article
- UvrC Coordinates an OJournal of the American Chemical Society · 2020Article
- The iron-sulphur cluster in human DNA2 is required for all biochemical activities of DNA2.Communications biology · 2020Article
- The l-Thr Kinase/l-Thr-Phosphate Decarboxylase (CobD) Enzyme fromBiochemistry · 2019Article
- Redox Chemistry in the Genome: Emergence of the [4Fe4S] Cofactor in Repair and Replication.Annual review of biochemistry · 2019Review
- Nitric Oxide Modulates Endonuclease III Redox Activity by a 800 mV Negative Shift upon [FeJournal of the American Chemical Society · 2018Article
- Comprehensive Analysis of the Global Protein Changes That Occur During Salivary Gland Degeneration in Female Ixodid TicksFrontiers in physiology · 2018Article
- A Redox Role for the [4Fe4S] Cluster of Yeast DNA Polymerase δ.Journal of the American Chemical Society · 2017Article
- Mechanistic and biological considerations of oxidatively damaged DNA for helicase-dependent pathways of nucleic acid metabolism.Free radical biology & medicine · 2017Review
- Electrochemistry of the [4Fe4S] Cluster in Base Excision Repair Proteins: Tuning the Redox Potential with DNA.Langmuir : the ACS journal of surfaces and colloids · 2017Article
- Article
- Electrical Probes of DNA-Binding Proteins.Methods in enzymology · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Escherichia coli DNA damage-inducible protein DinG, a member of the superfamily 2 DNA helicases, has been implicated in the nucleotide excision repair and recombinational DNA repair pathways. Combining UV-visible absorption, EPR, and enzyme activity measurements, we demonstrate here that E. coli DinG contains a redox-active [4Fe-4S] cluster with a midpoint redox potential (E(m)) of -390 +/- 23 mV (pH 8.0) and that reduction of the [4Fe-4S] cluster reversibly switches off the DinG helicase activity. Unlike the [4Fe-4S] cluster in E. coli dihydroxyacid dehydratase, the DinG [4Fe-4S] cluster is stable, and the enzyme remains fully active after exposure to 100-fold excess of hydrogen peroxide, indicating that DinG could be functional under oxidative stress conditions. However, the DinG [4Fe-4S] cluster can be efficiently modified by nitric oxide (NO), forming the DinG-bound dinitrosyl iron complex with the concomitant inactivation of helicase activity in vitro and in vivo. Reassembly of the [4Fe-4S] cluster in NO-modified DinG restores helicase activity, indicating that the iron-sulfur cluster in DinG is the primary target of NO cytotoxicity. The results led us to propose that the iron-sulfur cluster in DinG may act as a sensor of intracellular redox potential to modulate its helicase activity and that modification of the iron-sulfur cluster in DinG and likely in other DNA repair enzymes by NO may contribute to NO-mediated genomic instability.
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