ArticleNucleic acids research2023
CasDinG is a 5'-3' dsDNA and RNA/DNA helicase with three accessory domains essential for type IV CRISPR immunity.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Structural and biochemical characterization of a novel DinG containing an endonuclease domain.Cellular and molecular life sciences : CMLS · 2026Article
- Delivering a multi-color, cell-based CRISPR experience to low-resource classrooms.Journal of microbiology & biology education · 2026Article
- The DinG exonuclease acts as a primary quality controller to remove unprocessed ribosomal RNAs.Nucleic acids research · 2026Article
- Type I-Fv and engineered type IV-A1 CRISPR-Cas effectors facilitate genome reduction in Escherichia coli.Nucleic acids research · 2025Article
- Characterization and engineering of a type IV-A3 CRISPR-Cas system for genome editing in Escherichia coli.Nucleic acids research · 2025Article
- Article
- Determining the biochemical function of type IV CRISPR ribonucleoprotein complexes and accessory proteins.Methods in enzymology · 2025Article
- Emerging tools in plant genome editing.Frontiers in genome editing · 2025Review
- Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025Review
- Article
- Visualization of Type IV-A1 CRISPR-mediated repression of gene expression and plasmid replication.Nucleic acids research · 2024Article
- Hachiman is a genome integrity sensor.bioRxiv : the preprint server for biology · 2024Article
- The N-terminal domain of Type IV-A1 CRISPR-associated DinG is vulnerable to proteolysis.microPublication biology · 2024Article
- Uncovering the functional diversity of rare CRISPR-Cas systems with deep terascale clustering.Science (New York, N.Y.) · 2023Article
- The biology and type I/III hybrid nature of type I-D CRISPR-Cas systems.The Biochemical journal · 2023Review
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Authors and funding
7 authors.
Funding
Abstract
CRISPR-associated DinG protein (CasDinG) is essential to type IV-A CRISPR function. Here, we demonstrate that CasDinG from Pseudomonas aeruginosa strain 83 is an ATP-dependent 5'-3' DNA translocase that unwinds double-stranded (ds)DNA and RNA/DNA hybrids. The crystal structure of CasDinG reveals a superfamily 2 helicase core of two RecA-like domains with three accessory domains (N-terminal, arch, and vestigial FeS). To examine the in vivo function of these domains, we identified the preferred PAM sequence for the type IV-A system (5'-GNAWN-3' on the 5'-side of the target) with a plasmid library and performed plasmid clearance assays with domain deletion mutants. Plasmid clearance assays demonstrated that all three domains are essential for type IV-A immunity. Protein expression and biochemical assays suggested the vFeS domain is needed for protein stability and the arch for helicase activity. However, deletion of the N-terminal domain did not impair ATPase, ssDNA binding, or helicase activities, indicating a role distinct from canonical helicase activities that structure prediction tools suggest involves interaction with dsDNA. This work demonstrates CasDinG helicase activity is essential for type IV-A CRISPR immunity as well as the yet undetermined activity of the CasDinG N-terminal domain.
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