ArticleScience (New York, N.Y.)2025
Deazaguanylation is a nucleobase-protein conjugation required for type IV CBASS immunity.
Article in Science (New York, N.Y.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Structural and functional insights into QueC-family protein in QatABCD anti-phage system.Nature communications · 2026Article
- Functional divergence and conservation in the QueC protein family (PF06508): from tRNA modification to anti-phage defense.The Biochemical journal · 2026Article
- Review
- Recent Advances in the Molecular Mechanisms of Bacterial Anti-Phage Defence Systems.Microbial biotechnology · 2026Article
- Structural and enzymatic insights into QatD, a dual-function TatD-like nuclease in the QatABCD anti-phage defense system.Nucleic acids research · 2026Article
- Structural investigation of QatB and QatC proteins in QatABCD anti-phage defense.Nature communications · 2026Article
- Structural basis of QueC-family protein function in qatABCD anti-phage defense.Nature communications · 2026Article
- Functional Divergence and Conservation in the QueC Protein Family (PF06508): From tRNA Modification to Anti-Phage Defense.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of QueC-family protein function in qatABCD anti-phage defense.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
- Update of
Authors and funding
6 authors.
Funding
Abstract
7-Deazapurines are nucleobase analogs essential for nucleic acid modifications in nearly all cellular life. In this study, we discovered a role for 7-deazapurines in protein modification within type IV cyclic oligonucleotide-based antiviral signaling system (CBASS) antiphage defense and defined functions for CBASS ancillary proteins Cap9 and Cap10 in nucleobase-protein conjugation. A structure of Cap10 revealed a transfer RNA transglycosylase family enzyme remodeled to bind a partner cGAS/DncV-like nucleotidyltransferase that is modified with an N-terminal 7-amido-7-deazaguanine (NDG) nucleobase. A structure of Cap9 explained how this QueC-like enzyme co-opts a 7-deazapurine biosynthetic reaction to install NDG. We show that Cap9, Cap10, and protein deazaguanylation are essential for host defense against phage infection. Our results define a 7-deazapurine protein modification and explain how nucleobase biosynthetic machinery has been repurposed for antiviral immunity.
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Registered trials
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 Socratic graph.