Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6

Upon target RNA recognition, type III CRISPR-Cas systems produce cyclic oligoadenylates that activate effectors such as Csm6 ribonucleases. Here, Garcia-Doval et al. show that Enteroccocus italicus Csm6 degrades its cyclic hexa-AMP activator, and report the crystal structure of the protein bound to...

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Main Authors: Carmela Garcia-Doval, Frank Schwede, Christian Berk, Jakob T. Rostøl, Ole Niewoehner, Oliver Tejero, Jonathan Hall, Luciano A. Marraffini, Martin Jinek
Format: Article
Language:English
Published: Nature Portfolio 2020-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-15334-5
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author Carmela Garcia-Doval
Frank Schwede
Christian Berk
Jakob T. Rostøl
Ole Niewoehner
Oliver Tejero
Jonathan Hall
Luciano A. Marraffini
Martin Jinek
author_facet Carmela Garcia-Doval
Frank Schwede
Christian Berk
Jakob T. Rostøl
Ole Niewoehner
Oliver Tejero
Jonathan Hall
Luciano A. Marraffini
Martin Jinek
author_sort Carmela Garcia-Doval
collection DOAJ
description Upon target RNA recognition, type III CRISPR-Cas systems produce cyclic oligoadenylates that activate effectors such as Csm6 ribonucleases. Here, Garcia-Doval et al. show that Enteroccocus italicus Csm6 degrades its cyclic hexa-AMP activator, and report the crystal structure of the protein bound to an activator mimic.
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spelling doaj.art-72db17b42bde4a3aab3bcb1de11e229a2022-12-21T19:26:57ZengNature PortfolioNature Communications2041-17232020-03-011111910.1038/s41467-020-15334-5Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6Carmela Garcia-Doval0Frank Schwede1Christian Berk2Jakob T. Rostøl3Ole Niewoehner4Oliver Tejero5Jonathan Hall6Luciano A. Marraffini7Martin Jinek8Department of Biochemistry, University of ZurichBiolog Life Science Institute GmbH & Co. KGDepartment of Chemistry and Applied Biosciences, Institute for Pharmaceutical Sciences, ETH ZurichLaboratory of Bacteriology, The Rockefeller UniversityDepartment of Biochemistry, University of ZurichDepartment of Biochemistry, University of ZurichDepartment of Chemistry and Applied Biosciences, Institute for Pharmaceutical Sciences, ETH ZurichLaboratory of Bacteriology, The Rockefeller UniversityDepartment of Biochemistry, University of ZurichUpon target RNA recognition, type III CRISPR-Cas systems produce cyclic oligoadenylates that activate effectors such as Csm6 ribonucleases. Here, Garcia-Doval et al. show that Enteroccocus italicus Csm6 degrades its cyclic hexa-AMP activator, and report the crystal structure of the protein bound to an activator mimic.https://doi.org/10.1038/s41467-020-15334-5
spellingShingle Carmela Garcia-Doval
Frank Schwede
Christian Berk
Jakob T. Rostøl
Ole Niewoehner
Oliver Tejero
Jonathan Hall
Luciano A. Marraffini
Martin Jinek
Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6
Nature Communications
title Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6
title_full Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6
title_fullStr Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6
title_full_unstemmed Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6
title_short Activation and self-inactivation mechanisms of the cyclic oligoadenylate-dependent CRISPR ribonuclease Csm6
title_sort activation and self inactivation mechanisms of the cyclic oligoadenylate dependent crispr ribonuclease csm6
url https://doi.org/10.1038/s41467-020-15334-5
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