ArticleThe Journal of biological chemistry2014
Mycobacterium tuberculosis DinG is a structure-specific helicase that unwinds G4 DNA: implications for targeting G4 DNA as a novel therapeutic approach.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 53 citations in OpenAlex.
- Non-Random Distribution of G-Quadruplex Structures Reveals Regulatory and Ecological Adaptations in Bacterial Genomes.International journal of molecular sciences · 2025Article
- CUT&Tag reveals unconventional G-quadruplex landscape in Mycobacterium tuberculosis in response to oxidative stress.Nature communications · 2025Article
- Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025Review
- Prominent transcriptomic changes in Mycobacterium intracellulare under acidic and oxidative stress.BMC genomics · 2024Article
- Combating multidrug-resistance inNAR molecular medicine · 2024Article
- Exploring the G-quadruplex binding and unwinding activity of the bacterial FeS helicase DinG.Scientific reports · 2023Article
- Article
- Identification and characterisation of G-quadruplex DNA-forming sequences in theRSC chemical biology · 2023Article
- Genome-Wide Transcriptional Response ofFrontiers in microbiology · 2022Article
- Extracellular vesicles and immunogenic stress in cancer.Cell death & disease · 2021Review
- Genetic Analysis of DinG Family Helicase YoaA and Its Interaction with Replication Clamp Loader Protein HolC in Escherichia coli.Journal of bacteriology · 2021Article
- G-Quadruplex Structures in Bacteria: Biological Relevance and Potential as an Antimicrobial Target.Journal of bacteriology · 2021Review
- 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
- Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability.Microorganisms · 2020Article
- G-Quadruplexes in the Archaea Domain.Biomolecules · 2020Article
- E. coli Rep helicase and RecA recombinase unwind G4 DNA and are important for resistance to G4-stabilizing ligands.Nucleic acids research · 2020Article
- Antigenic Variation inJournal of bacteriology · 2020Article
- Changing of the guard: How the Lyme disease spirochete subverts the host immune response.The Journal of biological chemistry · 2020Review
- Surface Dependent Dual Recognition of a G-quadruplex DNA With Neomycin-Intercalator Conjugates.Frontiers in chemistry · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The significance of G-quadruplexes and the helicases that resolve G4 structures in prokaryotes is poorly understood. The Mycobacterium tuberculosis genome is GC-rich and contains >10,000 sequences that have the potential to form G4 structures. In Escherichia coli, RecQ helicase unwinds G4 structures. However, RecQ is absent in M. tuberculosis, and the helicase that participates in G4 resolution in M. tuberculosis is obscure. Here, we show that M. tuberculosis DinG (MtDinG) exhibits high affinity for ssDNA and ssDNA translocation with a 5' → 3' polarity. Interestingly, MtDinG unwinds overhangs, flap structures, and forked duplexes but fails to unwind linear duplex DNA. Our data with DNase I footprinting provide mechanistic insights and suggest that MtDinG is a 5' → 3' polarity helicase. Notably, in contrast to E. coli DinG, MtDinG catalyzes unwinding of replication fork and Holliday junction structures. Strikingly, we find that MtDinG resolves intermolecular G4 structures. These data suggest that MtDinG is a multifunctional structure-specific helicase that unwinds model structures of DNA replication, repair, and recombination as well as G4 structures. We finally demonstrate that promoter sequences of M. tuberculosis PE_PGRS2, mce1R, and moeB1 genes contain G4 structures, implying that G4 structures may regulate gene expression in M. tuberculosis. We discuss these data and implicate targeting G4 structures and DinG helicase in M. tuberculosis could be a novel therapeutic strategy for culminating the infection with this pathogen.
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