ArticleNucleic acids research2022
Target RNA-guided protease activity in type III-E CRISPR-Cas system.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Application and Research Prospects of CRISPR/Cas Gene Editing Technology in Lactic Acid Bacteria.Microorganisms · 2026Review
- Structural basis for regulation of a CBASS-CRISPR-Cas defense island by a transmembrane anti-σ factor and its ECF σ partner.Science advances · 2024Article
- Article
- CRISPR technology in human diseases.MedComm · 2024Review
- Molecular and structural basis of an ATPase-nuclease dual-enzyme anti-phage defense complex.Cell research · 2024Article
- Craspase Orthologs Cleave a Nonconserved Site in Target Protein Csx30.ACS chemical biology · 2024Article
- Structural basis of negative regulation of CRISPR-Cas7-11 by TPR-CHAT.Signal transduction and targeted therapy · 2024Article
- Harnessing CRISPR-Cas adaptation for RNA recording and beyond.BMB reports · 2024Review
- Discovery of Diverse CRISPR-Cas Systems and Expansion of the Genome Engineering Toolbox.Biochemistry · 2023Review
- An archaeal virus-encoded anti-CRISPR protein inhibits type III-B immunity by inhibiting Cas RNP complex turnover.Nucleic acids research · 2023Article
- A review on CRISPR/Cas: a versatile tool for cancer screening, diagnosis, and clinic treatment.Functional & integrative genomics · 2023Review
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type III-E CRISPR-Cas systems are newly identified adaptive immune systems in prokaryotes that use a single Cas7-11 protein to specifically cleave target RNA. Cas7-11 could associate with Csx29, a putative caspase-like protein encoded by the gene frequently found in the type III-E loci, suggesting a functional linkage between the RNase and protease activities in type III-E systems. Here, we demonstrated that target RNA recognition would stimulate the proteolytic activity of Csx29, and protein Csx30 is the endogenous substrate. More interestingly, while the cognate target RNA recognition would activate Csx29, non-cognate target RNA with the complementary 3' anti-tag sequence inhibits the enzymatic activity. Csx30 could bind to the sigma factor RpoE, which may initiate the stress response after proteolytic cleavage. Combined with biochemical and structural studies, we have elucidated the mechanisms underlying the target RNA-guided proteolytic activity of Csx29. Our work will guide further developments leveraging this simple RNA targeting system for RNA and protein-related applications.
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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.