+Search query
-Structure paper
Title | Type III-B CRISPR-Cas cascade of proteolytic cleavages. |
---|---|
Journal, issue, pages | Science, Vol. 383, Issue 6682, Page 512-519, Year 2024 |
Publish date | Feb 2, 2024 |
Authors | Jurre A Steens / Jack P K Bravo / Carl Raymund P Salazar / Caglar Yildiz / Afonso M Amieiro / Stephan Köstlbacher / Stijn H P Prinsen / Ane S Andres / Constantinos Patinios / Andreas Bardis / Arjan Barendregt / Richard A Scheltema / Thijs J G Ettema / John van der Oost / David W Taylor / Raymond H J Staals / |
PubMed Abstract | The generation of cyclic oligoadenylates and subsequent allosteric activation of proteins that carry sensory domains is a distinctive feature of type III CRISPR-Cas systems. In this work, we ...The generation of cyclic oligoadenylates and subsequent allosteric activation of proteins that carry sensory domains is a distinctive feature of type III CRISPR-Cas systems. In this work, we characterize a set of associated genes of a type III-B system from that contains two caspase-like proteases, SAVED-CHAT and PCaspase (prokaryotic caspase), co-opted from a cyclic oligonucleotide-based antiphage signaling system (CBASS). Cyclic tri-adenosine monophosphate (AMP)-induced oligomerization of SAVED-CHAT activates proteolytic activity of the CHAT domains, which specifically cleave and activate PCaspase. Subsequently, activated PCaspase cleaves a multitude of proteins, which results in a strong interference phenotype in vivo in Taken together, our findings reveal how a CRISPR-Cas-based detection of a target RNA triggers a cascade of caspase-associated proteolytic activities. |
External links | Science / PubMed:38301007 |
Methods | EM (single particle) |
Resolution | 3.1 Å |
Structure data | EMDB-41358, PDB-8tl0: |
Source |
|
Keywords | IMMUNE SYSTEM / SAVED-CHAT |