ArticleNucleic acids research2020
Emergence of a novel immune-evasion strategy from an ancestral protein fold in bacteriophage Mu.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- An expanded realm of anti-CRISPR-associated proteins and regulatory mechanisms.Nucleic acids research · 2026Article
- Targeted DNA ADP-ribosylation triggers templated repair in bacteria and base mutagenesis in eukaryotes.Nature biotechnology · 2026Article
- A single viral enzyme drives tRNA-dependent hypermodification of DNA at adenine.Nature communications · 2026Article
- Simultaneous inhibition of bacterial virulence and anti-phage defense systems by synergistic bacteriophage counter-defense proteins.The EMBO journal · 2026Article
- Unveil the Secret of the Bacteria and Phage Arms Race.International journal of molecular sciences · 2023Review
- Evidence of a Set of Core-Function Genes in 16 Bacillus Podoviral Genomes with Considerable Genomic Diversity.Viruses · 2023Article
- Binding Affinity Quantifications of the Bacteriophage Mu DNA Modification Protein Mom Using Microscale Thermophoresis (MST).Bio-protocol · 2022Article
- Hypermodified DNA in Viruses of E. coli and Salmonella.EcoSal Plus · 2021Review
- Gcn5-RelatedFrontiers in molecular biosciences · 2021Article
- Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The broad host range bacteriophage Mu employs a novel 'methylcarbamoyl' modification to protect its DNA from diverse restriction systems of its hosts. The DNA modification is catalyzed by a phage-encoded protein Mom, whose mechanism of action is a mystery. Here, we characterized the co-factor and metal-binding properties of Mom and provide a molecular mechanism to explain 'methylcarbamoyl'ation of DNA by Mom. Computational analyses revealed a conserved GNAT (GCN5-related N-acetyltransferase) fold in Mom. We demonstrate that Mom binds to acetyl CoA and identify the active site. We discovered that Mom is an iron-binding protein, with loss of Fe2+/3+-binding associated with loss of DNA modification activity. The importance of Fe2+/3+ is highlighted by the colocalization of Fe2+/3+ with acetyl CoA within the Mom active site. Puzzlingly, acid-base mechanisms employed by >309,000 GNAT members identified so far, fail to support methylcarbamoylation of adenine using acetyl CoA. In contrast, free-radical chemistry catalyzed by transition metals like Fe2+/3+ can explain the seemingly challenging reaction, accomplished by collaboration between acetyl CoA and Fe2+/3+. Thus, binding to Fe2+/3+, a small but unprecedented step in the evolution of Mom, allows a giant chemical leap from ordinary acetylation to a novel methylcarbamoylation function, while conserving the overall protein architecture.
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