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A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT

Bacterial toxin-antitoxin (TA) modules are tightly regulated to maintain growth in favorable conditions or growth arrest during stress. A typical regulatory strategy involves the antitoxin binding and repressing its own promoter while the toxin often acts as a co-repressor. Here we show that Pseudom...

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Autores principales: Talavera, Ariel, Tamman, Hedvig, Ainelo, Andres, Konijnenberg, Albert, Hadži, San, Sobott, Frank, Garcia-Pino, Abel, Hõrak, Rita, Loris, Remy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6393540/
https://www.ncbi.nlm.nih.gov/pubmed/30814507
http://dx.doi.org/10.1038/s41467-019-08865-z
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author Talavera, Ariel
Tamman, Hedvig
Ainelo, Andres
Konijnenberg, Albert
Hadži, San
Sobott, Frank
Garcia-Pino, Abel
Hõrak, Rita
Loris, Remy
author_facet Talavera, Ariel
Tamman, Hedvig
Ainelo, Andres
Konijnenberg, Albert
Hadži, San
Sobott, Frank
Garcia-Pino, Abel
Hõrak, Rita
Loris, Remy
author_sort Talavera, Ariel
collection PubMed
description Bacterial toxin-antitoxin (TA) modules are tightly regulated to maintain growth in favorable conditions or growth arrest during stress. A typical regulatory strategy involves the antitoxin binding and repressing its own promoter while the toxin often acts as a co-repressor. Here we show that Pseudomonas putida graTA-encoded antitoxin GraA and toxin GraT differ from other TA proteins in the sense that not the antitoxin but the toxin possesses a flexible region. GraA auto-represses the graTA promoter: two GraA dimers bind cooperatively at opposite sides of the operator sequence. Contrary to other TA modules, GraT is a de-repressor of the graTA promoter as its N-terminal disordered segment prevents the binding of the GraT(2)A(2) complex to the operator. Removal of this region restores operator binding and abrogates Gr aT toxicity. GraTA represents a TA module where a flexible region in the toxin rather than in the antitoxin controls operon expression and toxin activity.
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spelling pubmed-63935402019-03-01 A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT Talavera, Ariel Tamman, Hedvig Ainelo, Andres Konijnenberg, Albert Hadži, San Sobott, Frank Garcia-Pino, Abel Hõrak, Rita Loris, Remy Nat Commun Article Bacterial toxin-antitoxin (TA) modules are tightly regulated to maintain growth in favorable conditions or growth arrest during stress. A typical regulatory strategy involves the antitoxin binding and repressing its own promoter while the toxin often acts as a co-repressor. Here we show that Pseudomonas putida graTA-encoded antitoxin GraA and toxin GraT differ from other TA proteins in the sense that not the antitoxin but the toxin possesses a flexible region. GraA auto-represses the graTA promoter: two GraA dimers bind cooperatively at opposite sides of the operator sequence. Contrary to other TA modules, GraT is a de-repressor of the graTA promoter as its N-terminal disordered segment prevents the binding of the GraT(2)A(2) complex to the operator. Removal of this region restores operator binding and abrogates Gr aT toxicity. GraTA represents a TA module where a flexible region in the toxin rather than in the antitoxin controls operon expression and toxin activity. Nature Publishing Group UK 2019-02-27 /pmc/articles/PMC6393540/ /pubmed/30814507 http://dx.doi.org/10.1038/s41467-019-08865-z Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Talavera, Ariel
Tamman, Hedvig
Ainelo, Andres
Konijnenberg, Albert
Hadži, San
Sobott, Frank
Garcia-Pino, Abel
Hõrak, Rita
Loris, Remy
A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT
title A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT
title_full A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT
title_fullStr A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT
title_full_unstemmed A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT
title_short A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT
title_sort dual role in regulation and toxicity for the disordered n-terminus of the toxin grat
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6393540/
https://www.ncbi.nlm.nih.gov/pubmed/30814507
http://dx.doi.org/10.1038/s41467-019-08865-z
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