ArticleNucleic acids research2018
Crystal structure of the modification-dependent SRA-HNH endonuclease TagI.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 18 citations in OpenAlex.
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- Argonaute-HNH filaments triggered by invader DNA confer bacterial immunity.Nature communications · 2025Article
- Structural analysis of the BisI family of modification dependent restriction endonucleases.Nucleic acids research · 2024Article
- Reappraisal of the DNA phosphorothioate modification machinery: uncovering neglected functional modalities and identification of new counter-invader defense systems.Nucleic acids research · 2024Article
- Functionally comparable but evolutionarily distinct nucleotide-targeting effectors help identify conserved paradigms across diverse immune systems.Nucleic acids research · 2023Article
- Identification and characterization of a new HNH restriction endonuclease with unusual properties.Applied microbiology and biotechnology · 2023Article
- A mobile restriction-modification system provides phage defence and resolves an epigenetic conflict with an antagonistic endonuclease.Nucleic acids research · 2022Article
- Crystal structures of the EVE-HNH endonuclease VcaM4I in the presence and absence of DNA.Nucleic acids research · 2021Article
- DNA backbone interactions impact the sequence specificity of DNA sulfur-binding domains: revelations from structural analyses.Nucleic acids research · 2020Article
- The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins.Journal of structural biology · 2020Article
- HK97 gp74 Possesses an α-Helical Insertion in the ββα Fold That Affects Its Metal Binding,Journal of bacteriology · 2020Article
- Crystal structure of the EcoKMcrA N-terminal domain (NEco): recognition of modified cytosine bases without flipping.Nucleic acids research · 2019Article
- A protein architecture guided screen for modification dependent restriction endonucleases.Nucleic acids research · 2019Article
- Type II Restriction of Bacteriophage DNA With 5hmdU-Derived Base Modifications.Frontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TagI belongs to the recently characterized SRA-HNH family of modification-dependent restriction endonucleases (REases) that also includes ScoA3IV (Sco5333) and TbiR51I (Tbis1). Here, we present a crystal structure of dimeric TagI, which exhibits a DNA binding site formed jointly by the nuclease domains, and separate binding sites for modified DNA bases in the two protomers. The nuclease domains have characteristic features of HNH/ββα-Me REases, and catalyze nicks or double strand breaks, with preference for /RY and RYN/RY sites, respectively. The SRA domains have the canonical fold. Their pockets for the flipped bases are spacious enough to accommodate 5-methylcytosine (5mC) or 5-hydroxymethylcytosine (5hmC), but not glucosyl-5-hydroxymethylcytosine (g5hmC). Such preference is in agreement with the biochemical determination of the TagI modification dependence and the results of phage restriction assays. The ability of TagI to digest plasmids methylated by Dcm (C5mCWGG), M.Fnu4HI (G5mCNGC) or M.HpyCH4IV (A5mCGT) suggests that the SRA domains of the enzyme are tolerant to different sequence contexts of the modified base.
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