2026-10-12T03:41:13Z https://data.mendeley.com/oai

oai:data.mendeley.com/drczc2m5mc.1 2024-10-02T09:17:22Z

Tamulaitis, Gintautas Filament formation activates protease and ring nuclease activities of CRISPR Lon-SAVED. Smalakyte et al. Mendeley Data To combat phage infection, type III CRISPR-Cas systems utilize cyclic oligoadenylates (cAn) signaling to activate various auxiliary effectors, including the CRISPR-associated Lon-SAVED protease CalpL, which forms a tripartite effector system together with an anti-σ factor, CalpT, and an ECF-like σ factor, CalpS. Here we report the characterization of the Candidatus Cloacimonas acidaminovorans CalpL-CalpT-CalpS. We demonstrate that cA4 binding triggers CalpL filament formation and activates it to cleave CalpT within the CalpT-CalpS dimer. This cleavage exposes the CalpT C-degron, which targets it for further degradation by cellular proteases. Consequently, CalpS is released to bind to RNA polymerase, causing growth arrest in E. coli. Furthermore, the CalpL-CalpT-CalpS system is regulated by the SAVED domain of CalpL, which is a ring nuclease that cleaves cA4 in a sequential three-step mechanism. These findings provide key mechanistic details for the activation, proteolytic events, and regulation of the signaling cascade in the type III CRISPR-Cas immunity. This dataset contains the original images of the gels, agar plates, and denoised cryo-EM micrographs from the paper "Filament formation activates protease and ring nuclease activities of CRISPR Lon-SAVED" published in Molecular Cell. Cryo-Electron Microscopy Escherichia coli Fluorescence Assay Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis Smalakyte, Dalia Ruksenaite, Audrone Sasnauskas, Giedrius Tamulaitiene, Giedre Dataset doi:10.17632/drczc2m5mc.1 oai:data.mendeley.com/drczc2m5mc.1 Creative Commons Attribution 4.0 International http://creativecommons.org/licenses/by/4.0 https://data.mendeley.com/datasets/drczc2m5mc 2024-10-02T09:17:22Z