ArticleScientific reports2015
Expression and purification of a single-chain Type IV restriction enzyme Eco94GmrSD and determination of its substrate preference.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 36 citations in OpenAlex.
- DNA modifications of Durham Collection phages and promiscuity of GmrSD-family Type IV restriction enzyme BrxU.Applied and environmental microbiology · 2026Article
- Biosynthesis of glycosylated 5-hydroxycytosine in the DNA of diverse viruses.Nucleic acids research · 2026Article
- A pair of DNA glucosyltransferases elevate counter-defense in bacteriophage T4.Nucleic acids research · 2026Article
- Type II Restriction of 2-Aminoadenosine (dZ)-Modified DNA and Production of dZ-Modified Plasmid inViruses · 2026Article
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- Defence systems encoded by core genomic islands of seventh pandemicPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Modified DNA substrate selectivity by GmrSD-family Type IV restriction enzyme BrxU.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Article
- West African-South American pandemic Vibrio cholerae encodes multiple distinct phage defence systems.Nature microbiology · 2025Article
- Molecular basis of the phosphorothioation-sensing antiphage defense system IscS-DndBCDE-DndI.Nucleic acids research · 2024Article
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- AJournal of bacteriology · 2024Article
- An enterococcal phage protein inhibits type IV restriction enzymes involved in antiphage defense.Nature communications · 2024Article
- An enterococcal phage protein broadly inhibits type IV restriction enzymes involved in antiphage defense.bioRxiv : the preprint server for biology · 2024Article
- A nuclease domain fused to the Snf2 helicase confers antiphage defence in coral-associated Halomonas meridiana.Microbial biotechnology · 2024Article
- AbioRxiv : the preprint server for biology · 2024Article
- Conserved domains can be found across distinct phage defence systems.Molecular microbiology · 2023Review
- Characterization of BisI Homologs.Frontiers in microbiology · 2021Article
- Expression of Human ACE2 N-terminal Domain, Part of the Receptor for SARS-CoV-2, in Fusion With Maltose-Binding Protein,Frontiers in microbiology · 2021Article
- SspABCD-SspE is a phosphorothioation-sensing bacterial defence system with broad anti-phage activities.Nature microbiology · 2020Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The first reported Type IV restriction endonuclease (REase) GmrSD consists of GmrS and GmrD subunits. In most bacteria, however, the gmrS and gmrD genes are fused together to encode a single-chain protein. The fused coding sequence for ECSTEC94C_1402 from E. coli strain STEC_94C was expressed in T7 Express. The protein designated as Eco94GmrSD displays modification-dependent ATP-stimulated REase activity on T4 DNA with glucosyl-5-hydroxymethyl-cytosines (glc-5hmC) and T4gt DNA with 5-hydroxymethyl-cytosines (5hmC). A C-terminal 6xHis-tagged protein was purified by two-column chromatography. The enzyme is active in Mg(2+) and Mn(2+) buffer. It prefers to cleave large glc-5hmC- or 5hmC-modified DNA. In phage restriction assays, Eco94GmrSD weakly restricted T4 and T4gt, whereas T4 IPI*-deficient phage (Δip1) were restricted more than 10(6)-fold, consistent with IPI* protection of E. coli DH10B from lethal expression of the closely homologous E. coli CT596 GmrSD. Eco94GmrSD is proposed to belong to the His-Asn-His (HNH)-nuclease family by the identification of a putative C-terminal REase catalytic site D507-H508-N522. Supporting this, GmrSD variants D507A, H508A, and N522A displayed no endonuclease activity. The presence of a large number of fused GmrSD homologs suggests that GmrSD is an effective phage exclusion protein that provides a mechanism to thwart T-even phage infection.
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