Chaperone addiction of toxin–antitoxin systems

Some bacterial toxin-antitoxin systems consist of a labile antitoxin that inhibits a toxin, and a chaperone that stabilizes the antitoxin. Here, Bordes et al. identify a sequence within the antitoxin to which the chaperone binds and which can be transferred to other proteins to make them chaperone-d...

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Main Authors: Patricia Bordes, Ambre Julie Sala, Sara Ayala, Pauline Texier, Nawel Slama, Anne-Marie Cirinesi, Valérie Guillet, Lionel Mourey, Pierre Genevaux
Format: Article
Language:English
Published: Nature Portfolio 2016-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms13339
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author Patricia Bordes
Ambre Julie Sala
Sara Ayala
Pauline Texier
Nawel Slama
Anne-Marie Cirinesi
Valérie Guillet
Lionel Mourey
Pierre Genevaux
author_facet Patricia Bordes
Ambre Julie Sala
Sara Ayala
Pauline Texier
Nawel Slama
Anne-Marie Cirinesi
Valérie Guillet
Lionel Mourey
Pierre Genevaux
author_sort Patricia Bordes
collection DOAJ
description Some bacterial toxin-antitoxin systems consist of a labile antitoxin that inhibits a toxin, and a chaperone that stabilizes the antitoxin. Here, Bordes et al. identify a sequence within the antitoxin to which the chaperone binds and which can be transferred to other proteins to make them chaperone-dependent.
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spelling doaj.art-f1097791d71b44849d1f858666413acb2022-12-21T19:27:28ZengNature PortfolioNature Communications2041-17232016-11-017111210.1038/ncomms13339Chaperone addiction of toxin–antitoxin systemsPatricia Bordes0Ambre Julie Sala1Sara Ayala2Pauline Texier3Nawel Slama4Anne-Marie Cirinesi5Valérie Guillet6Lionel Mourey7Pierre Genevaux8Laboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPSLaboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPSLaboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPSLaboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPSLaboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPSLaboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPSInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPSInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPSLaboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPSSome bacterial toxin-antitoxin systems consist of a labile antitoxin that inhibits a toxin, and a chaperone that stabilizes the antitoxin. Here, Bordes et al. identify a sequence within the antitoxin to which the chaperone binds and which can be transferred to other proteins to make them chaperone-dependent.https://doi.org/10.1038/ncomms13339
spellingShingle Patricia Bordes
Ambre Julie Sala
Sara Ayala
Pauline Texier
Nawel Slama
Anne-Marie Cirinesi
Valérie Guillet
Lionel Mourey
Pierre Genevaux
Chaperone addiction of toxin–antitoxin systems
Nature Communications
title Chaperone addiction of toxin–antitoxin systems
title_full Chaperone addiction of toxin–antitoxin systems
title_fullStr Chaperone addiction of toxin–antitoxin systems
title_full_unstemmed Chaperone addiction of toxin–antitoxin systems
title_short Chaperone addiction of toxin–antitoxin systems
title_sort chaperone addiction of toxin antitoxin systems
url https://doi.org/10.1038/ncomms13339
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AT nawelslama chaperoneaddictionoftoxinantitoxinsystems
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