ArticleNucleic acids research2024
Structural basis of Cas3 activation in type I-C CRISPR-Cas system.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Advances in CRISPR-Cas for Diagnosis and Treatment ofPathogens (Basel, Switzerland) · 2026Review
- Structural basis for dual mechanism of Cas2/3 nuclease inhibition by anti-CRISPR protein AcrIF19.Nature communications · 2026Article
- Structural basis of Cas8-independent Cas3 recruitment in Type I-F2 CRISPR-Cas.Nucleic acids research · 2026Article
- Antibody screening for tumor and immune hotspot targets: The frontier of new methods and technologies.Journal of pharmaceutical analysis · 2026Review
- Multilayer regulation of CRISPR systems: integrating anti-CRISPR proteins, CRISPRi/a, and quorum sensing networks.Frontiers in cellular and infection microbiology · 2026Review
- Structural basis of dimerization and cascade formation by Cas5.Scientific reports · 2025Article
- Structures reveal how the Cas1-2/3 integrase captures, delivers, and integrates foreign DNA into CRISPR loci.Structure (London, England : 1993) · 2025Article
- CRISPR/Cas-Based Ex Vivo Gene Therapy and Lysosomal Storage Disorders: A Perspective Beyond Cas9.Cells · 2025Review
- AcrIE7 inhibits the CRISPR-Cas system by directly binding to the R-loop single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Research Progress on the Mechanism and Application of the Type I CRISPR-Cas System.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
CRISPR-Cas systems function as adaptive immune mechanisms in bacteria and archaea and offer protection against phages and other mobile genetic elements. Among many types of CRISPR-Cas systems, Type I CRISPR-Cas systems are most abundant, with target interference depending on a multi-subunit, RNA-guided complex known as Cascade that recruits a transacting helicase nuclease, Cas3, to degrade the target. While structural studies on several other types of Cas3 have been conducted long ago, it was only recently that the structural study of Type I-C Cas3 in complex with Cascade was revealed, shedding light on how Cas3 achieve its activity in the Cascade complex. In the present study, we elucidated the first structure of standalone Type I-C Cas3 from Neisseria lactamica (NlaCas3). Structural analysis revealed that the histidine-aspartate (HD) nuclease active site of NlaCas3 was bound to two Fe2+ ions that inhibited its activity. Moreover, NlaCas3 could cleave both single-stranded and double-stranded DNA in the presence of Ni2+ or Co2+, showing the highest activity in the presence of both Ni2+ and Mg2+ ions. By comparing the structural studies of various Cas3 proteins, we determined that our NlaCas3 stays in an inactive conformation, allowing us to understand the structural changes associated with its activation and their implication.
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