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...
Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2016-11-01
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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. |
first_indexed | 2024-12-20T20:26:16Z |
format | Article |
id | doaj.art-f1097791d71b44849d1f858666413acb |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-20T20:26:16Z |
publishDate | 2016-11-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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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