Structural highlights
FunctionPublication Abstract from PubMedThe evolutionary arms race between bacteria and phages drives the development of bacterial antiviral defense systems and phage counter-defense strategies. Restriction-modification (RM) systems protect bacteria by methylating 'self' DNA and cleaving unmodified phage DNA. Phages like T-even coliphages evade RM systems by substituting cytosine with 5-hydroxymethyl cytosine (5hmC) or 5-glucosylated hmC (5ghmC). Here, we characterize âa single-component antiviral defense system featuring a GIY-YIG endonuclease domain. Biochemical and structural analyses demonstrate that this defense system is a type IV modification-dependent restriction endonuclease that specifically degrades 5hmC- or 5ghmC-modified DNA, and we accordingly name it CMoRE (Cytosine Modification âRâestriction Endonuclease). The crystal structures reveal an N-terminal GIY-YIG nuclease domain and a C-terminal modification-sensing domain. Unique features, including a 'GIYxY-YIG' motif and an inhibitory negatively charged loop, distinguish CMoRE as an additional member of the GIY-YIG family. This system not only highlights the evolutionary interplay between phages and bacteria but also presents CMoRE as a potential tool for precise genomic detection of 5hmC in mammals, with implications for epigenetics research and disease diagnostics. A bacterial defense system targeting modified cytosine of phage genomic DNA.,Liu R, Tang D, Niu M, Lei S, Zong Z, Chen Q, Yu Y Nat Commun. 2026 Jan 22. doi: 10.1038/s41467-026-68792-8. PMID:41571690[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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