ArticleNature communications2017
High-fidelity DNA replication in Mycobacterium tuberculosis relies on a trinuclear zinc center.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Diversity and distribution of bacterial DNA polymerases.Nucleic acids research · 2026Article
- Identification of determinants of high-fidelity DNA synthesis in Mycobacterium smegmatis DnaE1 through in silico and in vivo approaches.Nucleic acids research · 2025Article
- A unique inhibitor conformation selectively targets the DNA polymerase PolC of Gram-positive priority pathogens.Nature communications · 2025Article
- Revolutionizing tuberculosis treatment: Breakthroughs, challenges, and hope on the horizon.Acta pharmaceutica Sinica. B · 2025Review
- Genome editing outcomes reveal mycobacterial NucS participates in a short-patch repair of DNA mismatches.Nucleic acids research · 2024Article
- Genome Editing Outcomes Reveal Mycobacterial NucS Participates in a Short-Patch Repair of DNA Mismatches.bioRxiv : the preprint server for biology · 2023Article
- Engineering of the DNA replication and repair machinery to develop binary mutators for rapid genome evolution of Corynebacterium glutamicum.Nucleic acids research · 2023Article
- Molecular basis of RanGTP-activated release of Histones H2A-H2B from Importin-9.Structure (London, England : 1993) · 2023Article
- High-Throughput Exonuclease Assay Based on the Fluorescent Base Analogue 2-Aminopurine.ACS omega · 2023Article
- Molecular basis of RanGTP-activated nucleosome assembly with Histones H2A-H2B bound to Importin-9.bioRxiv : the preprint server for biology · 2023Article
- Hit Compounds and Associated Targets in IntracellularMolecules (Basel, Switzerland) · 2022Article
- DNA-Dependent Binding of Nargenicin to DnaE1 Inhibits Replication inACS infectious diseases · 2022Article
- Structural basis for recognition of distinct deaminated DNA lesions by endonuclease Q.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Novel Antibiotics Targeting Bacterial Replicative DNA Polymerases.Antibiotics (Basel, Switzerland) · 2020Review
- Mycobacterial DNA polymerase I: activities and crystal structures of the POL domain as apoenzyme and in complex with a DNA primer-template and of the full-length FEN/EXO-POL enzyme.Nucleic acids research · 2020Article
- Specificity and mutagenesis bias of the mycobacterial alternative mismatch repair analyzed by mutation accumulation studies.Science advances · 2020Article
- The Genetic Background Modulates the Evolution of Fluoroquinolone-Resistance in Mycobacterium tuberculosis.Molecular biology and evolution · 2020Article
- An array of basic residues is essential for the nucleolytic activity of the PHP domain of bacterial/archaeal PolX DNA polymerases.Scientific reports · 2019Article
- Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments.Nature methods · 2019Review
- DnaG Primase-A Target for the Development of Novel Antibacterial Agents.Antibiotics (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
High-fidelity DNA replication depends on a proofreading 3'-5' exonuclease that is associated with the replicative DNA polymerase. The replicative DNA polymerase DnaE1 from the major pathogen Mycobacterium tuberculosis (Mtb) uses its intrinsic PHP-exonuclease that is distinct from the canonical DEDD exonucleases found in the Escherichia coli and eukaryotic replisomes. The mechanism of the PHP-exonuclease is not known. Here, we present the crystal structure of the Mtb DnaE1 polymerase. The PHP-exonuclease has a trinuclear zinc center, coordinated by nine conserved residues. Cryo-EM analysis reveals the entry path of the primer strand in the PHP-exonuclease active site. Furthermore, the PHP-exonuclease shows a striking similarity to E. coli endonuclease IV, which provides clues regarding the mechanism of action. Altogether, this work provides important insights into the PHP-exonuclease and reveals unique properties that make it an attractive target for novel anti-mycobacterial drugs.The polymerase and histidinol phosphatase (PHP) domain in the DNA polymerase DnaE1 is essential for mycobacterial high-fidelity DNA replication. Here, the authors determine the DnaE1 crystal structure, which reveals the PHP-exonuclease mechanism that can be exploited for antibiotic development.
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