ArticleRNA biology2019
Biochemical analysis of the Cas6-1 RNA endonuclease associated with the subtype I-D CRISPR-Cas system in Synechocystis sp. PCC 6803.
Article in RNA biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Characterization of Five CRISPR Systems inInternational journal of molecular sciences · 2025Article
- Cyanobacterial type I CRISPR-Cas systems: distribution, mechanisms, and genome editing applications.Frontiers in bioengineering and biotechnology · 2025Review
- Research Progress on the Mechanism and Application of the Type I CRISPR-Cas System.International journal of molecular sciences · 2024Review
- Develop a Compact RNA Base Editor by Fusing ADAR with Engineered EcCas6e.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- The biology and type I/III hybrid nature of type I-D CRISPR-Cas systems.The Biochemical journal · 2023Review
- Adaptive laboratory evolution of a thermophile toward a reduced growth temperature optimum.Frontiers in microbiology · 2023Article
- Genome editing in mammalian cells using the CRISPR type I-D nuclease.Nucleic acids research · 2021Article
- Endogenous Type I CRISPR-Cas: From Foreign DNA Defense to Prokaryotic Engineering.Frontiers in bioengineering and biotechnology · 2020Review
- Article
- Divergent methylation of CRISPR repeats and cas genes in a subtype I-D CRISPR-Cas-system.BMC microbiology · 2019Article
- CRISPR-Cas systems in multicellular cyanobacteria.RNA biology · 2019Article
- CRISPR-Cas: more than ten years and still full of mysteries.RNA biology · 2019Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Specialized RNA endonucleases are critical for efficient activity of the CRISPR-Cas defense mechanisms against invading DNA or RNA. Cas6-type enzymes are the RNA endonucleases in many type I and type III CRISPR-Cas systems. These enzymes are diverse and critical residues involved in the recognition and cleavage of RNA substrates are not universally conserved. Cas6 endonucleases associated with the CRISPR-Cas subtypes I-A, I-B, I-C, I-E and I-F, as well as III-B have been studied from three archaea and four bacteria thus far. However, until now information about subtype I-D specific Cas6 endonucleases has remained scarce. Here, we report the biochemical analysis of Cas6-1, which is specific for the crRNA maturation from the subtype I-D CRISPR-Cas system of Synechocystis sp. PCC 6803. Assays of turnover kinetics suggest a single turnover mechanism for Cas6-1. The mutation of conserved amino acids R29A, H32A-S33A and H51A revealed these as essential, whereas the parallel mutation of R175A-R176A led to a pronounced and the K155A mutation to a slight reduction in enzymatic activity. In contrast, the mutations R67A, R81A and K231A left the enzymatic activity unchanged. These results are in accordance with the predominant role of histidine residues in the active site and of positively charged residues in RNA binding. Nevertheless, the protein-RNA interaction site seems to differ from other known systems, since imidazole could not restore the mutated histidine site.
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