ArticleNature structural & molecular biology2023
Structural insights into the regulation of Cas7-11 by TPR-CHAT.
Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Craspase Protease Activation Is Sensitive to Oncogenic Single-Nucleotide RNA Mismatches.ACS chemical biology · 2026Article
- Synthetic Type III-E CRISPR-Cas Effectors for Programmable RNA-targeting.Journal of molecular biology · 2026Article
- CRISPR-Cas opens a new era of antimicrobial therapy as a powerful gene editing tool.World journal of microbiology & biotechnology · 2025Review
- CRISPR RNA binding drives structural ordering that primes Cas7-11 for target cleavage.Nucleic acids research · 2025Article
- 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
- An archaeal virus-encoded anti-CRISPR protein inhibits type III-B immunity by inhibiting Cas RNP complex turnover.Nucleic acids research · 2023Article
- CRISPR-Cas has a new juggling act: interplay between nuclease and protease.Nature structural & molecular biology · 2023Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CRISPR-guided caspase (Craspase) complex is an assembly of the target-specific RNA nuclease known as Cas7-11 bound to CRISPR RNA (crRNA) and an ancillary protein known as TPR-CHAT (tetratricopeptide repeats (TPR) fused with a CHAT domain). The Craspase complex holds promise as a tool for gene therapy and biomedical research, but its regulation is poorly understood. TPR-CHAT regulates Cas7-11 nuclease activity via an unknown mechanism. In the present study, we use cryoelectron microscopy to determine structures of the Desulfonema magnum (Dm) Craspase complex to gain mechanistic insights into its regulation. We show that DmTPR-CHAT stabilizes crRNA-bound DmCas7-11 in a closed conformation via a network of interactions mediated by the DmTPR-CHAT N-terminal domain, the DmCas7-11 insertion finger and Cas11-like domain, resulting in reduced target RNA accessibility and cleavage.
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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.