ArticleNature communications2024
Structural variation of types IV-A1- and IV-A3-mediated CRISPR interference.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Structural basis of Cas8-independent Cas3 recruitment in Type I-F2 CRISPR-Cas.Nucleic acids research · 2026Article
- CRISPR-Cas is beneficial in plasmid competition, but limited by competitor toxin-antitoxin activity when horizontally transferred.PLoS biology · 2026Article
- Precision gene editing: The power of CRISPR-Cas in modern genetics.Molecular therapy. Nucleic acids · 2025Review
- 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
- Intricate interplay of CRISPR-Cas systems, anti-CRISPR proteins, and antimicrobial resistance genes in a globally successful multi-drug resistant Klebsiella pneumoniae clone.Genome medicine · 2025Article
- Emerging tools in plant genome editing.Frontiers in genome editing · 2025Review
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
CRISPR-Cas mediated DNA-interference typically relies on sequence-specific binding and nucleolytic degradation of foreign genetic material. Type IV-A CRISPR-Cas systems diverge from this general mechanism, using a nuclease-independent interference pathway to suppress gene expression for gene regulation and plasmid competition. To understand how the type IV-A system associated effector complex achieves this interference, we determine cryo-EM structures of two evolutionarily distinct type IV-A complexes (types IV-A1 and IV-A3) bound to cognate DNA-targets in the presence and absence of the type IV-A signature DinG effector helicase. The structures reveal how the effector complexes recognize the protospacer adjacent motif and target-strand DNA to form an R-loop structure. Additionally, we reveal differences between types IV-A1 and IV-A3 in DNA interactions and structural motifs that allow for in trans recruitment of DinG. Our study provides a detailed view of type IV-A mediated DNA-interference and presents a structural foundation for engineering type IV-A-based genome editing tools.
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