ArticleThe Journal of biological chemistry2011
Structural and biochemical analysis of nuclease domain of clustered regularly interspaced short palindromic repeat (CRISPR)-associated protein 3 (Cas3).
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
73 citing papers in PubMed, 125 citations in OpenAlex.
- Reconstructing the complex architecture of the genome with molecular scissors: applying genome editing technology in precision medicine.Frontiers in genome editing · 2026Review
- Assessing spacer acquisition rates inFrontiers in microbiology · 2024Article
- Article
- Characterization of the self-targeting Type IV CRISPR interference system in Pseudomonas oleovorans.Nature microbiology · 2022Article
- Anti-CRISPR proteins function through thermodynamic tuning and allosteric regulation of CRISPR RNA-guided surveillance complex.Nucleic acids research · 2022Article
- Dynamic mechanisms of CRISPR interference by Escherichia coli CRISPR-Cas3.Nature communications · 2022Article
- Metal Dependence and Functional Diversity of Type I Cas3 Nucleases.Biochemistry · 2022Article
- Article
- A Tryptophan 'Gate' in the CRISPR-Cas3 Nuclease Controls ssDNA Entry into the Nuclease Site, That When Removed Results in Nuclease Hyperactivity.International journal of molecular sciences · 2021Article
- Positioning Diverse Type IV Structures and Functions Within Class 1 CRISPR-Cas Systems.Frontiers in microbiology · 2021Article
- Structural basis for inhibition of an archaeal CRISPR-Cas type I-D large subunit by an anti-CRISPR protein.Nature communications · 2020Article
- Heavily Armed Ancestors: CRISPR Immunity and Applications in Archaea with a Comparative Analysis of CRISPR Types in Sulfolobales.Biomolecules · 2020Review
- HD-[HD-GYP] Phosphodiesterases: Activities and Evolutionary Diversification within the HD-GYP Family.Biochemistry · 2020Article
- Cas3/I-C mediated target DNA recognition and cleavage during CRISPR interference are independent of the composition and architecture of Cascade surveillance complex.Nucleic acids research · 2020Article
- Review
- Types I and V Anti-CRISPR Proteins: From Phage Defense to Eukaryotic Synthetic Gene Circuits.Frontiers in bioengineering and biotechnology · 2020Review
- Endogenous Type I CRISPR-Cas: From Foreign DNA Defense to Prokaryotic Engineering.Frontiers in bioengineering and biotechnology · 2020Review
- DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island.Nucleic acids research · 2019Article
- Structure-Function Analysis of the Phosphoesterase Component of the Nucleic Acid End-Healing EnzymeJournal of bacteriology · 2019Article
- Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
RNA transcribed from clustered regularly interspaced short palindromic repeats (CRISPRs) protects many prokaryotes from invasion by foreign DNA such as viruses, conjugative plasmids, and transposable elements. Cas3 (CRISPR-associated protein 3) is essential for this CRISPR protection and is thought to mediate cleavage of the foreign DNA through its N-terminal histidine-aspartate (HD) domain. We report here the 1.8 Å crystal structure of the HD domain of Cas3 from Thermus thermophilus HB8. Structural and biochemical studies predict that this enzyme binds two metal ions at its active site. We also demonstrate that the single-stranded DNA endonuclease activity of this T. thermophilus domain is activated not by magnesium but by transition metal ions such as manganese and nickel. Structure-guided mutagenesis confirms the importance of the metal-binding residues for the nuclease activity and identifies other active site residues. Overall, these results provide a framework for understanding the role of Cas3 in the CRISPR system.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.