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

Abstract

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 GraT2A2 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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Item Type:	Article
Authors/Creators:	Talavera, A Tamman, H Ainelo, A Konijnenberg, A Hadži, S Sobott, F https://orcid.org/0000-0001-9029-1865 Garcia-Pino, A Hõrak, R Loris, R
Copyright, Publisher and Additional Information:	© The Author(s) 2019. 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/.
Dates:	Accepted: 31 January 2019 Published (online): 27 February 2019 Published: 27 February 2019
Institution:	The University of Leeds
Academic Units:	The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds)
Depositing User:	Symplectic Publications
Date Deposited:	05 Mar 2019 13:58
Last Modified:	05 Mar 2019 13:58
Status:	Published
Publisher:	Nature Publishing Group
Identification Number:	10.1038/s41467-019-08865-z
Related URLs:	PubMed URL
Open Archives Initiative ID (OAI ID):	oai:eprints.whiterose.ac.uk:143220

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

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