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@ARTICLE{Rouillon:491620,
      author       = {Rouillon, Christophe and Schneberger, Niels and Chi,
                      Haotian and Blumenstock, Katja and Da Vela, Stefano and
                      Ackermann, Katrin and Moecking, Jonas and Peter, Martin and
                      Boenigk, Wolfgang and Seifert, Reinhard and Bode, Bela E.
                      and Schmid-Burgk, Jonathan L. and Svergun, Dmitri and Geyer,
                      Matthias and White, Malcolm F. and Hagelueken, Gregor},
      title        = {{A}ntiviral signalling by a cyclic nucleotide activated
                      {CRISPR} protease},
      journal      = {Nature},
      volume       = {614},
      number       = {7946},
      issn         = {0028-0836},
      address      = {London [u.a.]},
      publisher    = {Nature Publ. Group},
      reportid     = {PUBDB-2023-00312},
      pages        = {168 - 174},
      year         = {2022},
      abstract     = {CRISPR defence systems such as the well-known DNA-targeting
                      Cas9 and the RNA-targeting type III systems are widespread
                      in prokaryotes1,2. The latter orchestrates a complex
                      antiviral response that is initiated through the synthesis
                      of cyclic oligoadenylates after recognition of foreign
                      RNA3,4,5. Among the large set of proteins that are linked to
                      type III systems and predicted to bind cyclic
                      oligoadenylates6,7, a CRISPR-associated Lon protease (CalpL)
                      stood out to us. CalpL contains a sensor domain of the SAVED
                      family7 fused to a Lon protease effector domain. However,
                      the mode of action of this effector is unknown. Here we
                      report the structure and function of CalpL and show that
                      this soluble protein forms a stable tripartite complex with
                      two other proteins, CalpT and CalpS, that are encoded on the
                      same operon. After activation by cyclic tetra-adenylate
                      (cA4), CalpL oligomerizes and specifically cleaves the MazF
                      homologue CalpT, which releases the extracytoplasmic
                      function σ factor CalpS from the complex. Our data
                      provide a direct connection between CRISPR-based detection
                      of foreign nucleic acids and transcriptional regulation.
                      Furthermore, the presence of a SAVED domain that binds
                      cyclic tetra-adenylate in a CRISPR effector reveals a link
                      to the cyclic-oligonucleotide-based antiphage signalling
                      system.},
      cin          = {EMBL-User / EMBL},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)390873048 - EXC 2151: ImmunoSensation2 - the
                      immune sensory system (390873048)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)390873048},
      experiment   = {EXP:(DE-H253)P-P12-20150101 / EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36423657},
      UT           = {WOS:000912338800001},
      doi          = {10.1038/s41586-022-05571-7},
      url          = {https://bib-pubdb1.desy.de/record/491620},
}