ArticleiScience2018
Structural and Mechanistic Analyses Reveal a Unique Cas4-like Protein in the Mimivirus Virophage Resistance Element System.
Article in iScience, 2018. 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.
- The Viral AlphaFold Database of monomers and homodimers reveals conserved protein folds in viruses of bacteria, archaea, and eukaryotes.Science advances · 2025Article
- Structure and mechanism of the Red recombination system of bacteriophage λ.Progress in biophysics and molecular biology · 2019Review
- Virophages of Giant Viruses: An Update at Eleven.Viruses · 2019Review
- Giant Viruses-Big Surprises.Viruses · 2019Review
- Review
- Viva lavidaviruses! Five features of virophages that parasitize giant DNA viruses.PLoS pathogens · 2019Article
- Guarani Virophage, a New Sputnik-Like Isolate From a Brazilian Lake.Frontiers in microbiology · 2019Article
- Role of the R349 Gene and Its Repeats in the MIMIVIRE Defense System.Frontiers in microbiology · 2019Article
- CRISPR-Cas Systems and the Paradox of Self-Targeting Spacers.Frontiers in microbiology · 2019Review
- Ancestrality and Mosaicism of Giant Viruses Supporting the Definition of the Fourth TRUC of Microbes.Frontiers in microbiology · 2018Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A clustered regularly interspaced short palindromic repeats (CRISPR)-like "mimivirus virophage resistance element" (MIMIVIRE) system, which contains specific cascade genes and a CRISPR array against virophages, was reported in mimiviruses. An essential component of the MIMIVIRE system is R354, encoding a nuclease and a likely functional homolog of Cas4. Here we show that R354 is a dual nuclease with both exonuclease and endonuclease activities. Structural analysis revealed that the catalytic core domain of R354 is similar to those of Cas4 and ? exonuclease despite their low sequence identity. R354 forms a homodimer that is important for its exonuclease but not endonuclease activity. Structural comparisons between the active and semi-active states of R354 demonstrated that an activation loop adjacent to the catalytic site is critical for enzymatic activity. Overall, the results suggest that R354 belongs to a novel MIMIVIRE system involved in innate virus immunity and provides a template for the identification of new CRISPR systems in other species.
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