ArticleNucleic acids research2010
The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 71 citations in OpenAlex.
- DNA-Mimic Antirestriction Proteins ArdA Could Regulate Gene Expression inInternational journal of molecular sciences · 2026Article
- Co-occurrence of diverse defense systems shapes complex microbe-virus relationships in deep-sea cold seeps.Nature communications · 2026Article
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- BlihIA-A Novel Type I Restriction-Modification System fromInternational journal of molecular sciences · 2025Article
- Advances in Diversity, Evolutionary Dynamics and Biotechnological Potential of Restriction-Modification Systems.Microorganisms · 2025Review
- Article
- The role of leptospiral proteins in immune evasion and inflammatory response stimulation in HEK293T cell monolayers.Frontiers in immunology · 2025Article
- Various plasmid strategies limit the effect of bacterial restriction-modification systems against conjugation.Nucleic acids research · 2024Article
- Assessing the Role of Bacterial Innate and Adaptive Immunity as Barriers to Conjugative Plasmids.Molecular biology and evolution · 2024Article
- CRISPR-Cas3 and type I restriction-modification team up against blaBMC microbiology · 2024Article
- RecA-dependent or independent recombination of plasmid DNA generates a conflict with the host EcoKI immunity by launching restriction alleviation.Nucleic acids research · 2024Article
- Inhibitors of bacterial immune systems: discovery, mechanisms and applications.Nature reviews. Genetics · 2024Review
- Accumulation of defense systems in phage-resistant strains ofScience advances · 2024Article
- Interrogating two extensively self-targeting Type I CRISPR-Cas systems in Xanthomonas albilineans reveals distinct anti-CRISPR proteins that block DNA degradation.Nucleic acids research · 2024Article
- dbAPIS: a database of anti-prokaryotic immune system genes.Nucleic acids research · 2024Article
- Isolation and draft genome sequence ofJournal of genomics · 2024Article
- The bacterial genetic determinants of Escherichia coli capacity to cause bloodstream infections in humans.PLoS genetics · 2023Article
- Conjugation's Toolkit: the Roles of Nonstructural Proteins in Bacterial Sex.Journal of bacteriology · 2023Review
- Broadness and specificity: ArdB, ArdA, and Ocr against various restriction-modification systems.Frontiers in microbiology · 2023Article
- Combined comparative genomics and clinical modeling reveals plasmid-encoded genes are independently associated with Klebsiella infection.Nature communications · 2022Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Plasmids, conjugative transposons and phage frequently encode anti-restriction proteins to enhance their chances of entering a new bacterial host that is highly likely to contain a Type I DNA restriction and modification (RM) system. The RM system usually destroys the invading DNA. Some of the anti-restriction proteins are DNA mimics and bind to the RM enzyme to prevent it binding to DNA. In this article, we characterize ArdB anti-restriction proteins and their close homologues, the KlcA proteins from a range of mobile genetic elements; including an ArdB encoded on a pathogenicity island from uropathogenic Escherichia coli and a KlcA from an IncP-1b plasmid, pBP136 isolated from Bordetella pertussis. We show that all the ArdB and KlcA act as anti-restriction proteins and inhibit the four main families of Type I RM systems in vivo, but fail to block the restriction endonuclease activity of the archetypal Type I RM enzyme, EcoKI, in vitro indicating that the action of ArdB is indirect and very different from that of the DNA mimics. We also present the structure determined by NMR spectroscopy of the pBP136 KlcA protein. The structure shows a novel protein fold and it is clearly not a DNA structural mimic.
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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.