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An oxygen-sensitive toxin–antitoxin system

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Title: An oxygen-sensitive toxin–antitoxin system
Authors: Marimon, O
Teixeira, JMC
Cordeiro, TN
Soo, VWC
Wood, TL
Mayzel, M
Amata, I
García, J
Morera, A
Gay, M
Vilaseca, M
Orekhov, VY
Wood, TK
Pons, M
Item Type: Journal Article
Abstract: The Hha and TomB proteins from Escherichia coli form an oxygen-dependent toxin–antitoxin (TA) system. Here we show that YmoB, the Yersinia orthologue of TomB, and its single cysteine variant [C117S]YmoB can replace TomB as antitoxins in E. coli. In contrast to other TA systems, [C117S]YmoB transiently interacts with Hha (rather than forming a stable complex) and enhances the spontaneous oxidation of the Hha conserved cysteine residue to a -SOxH-containing species (sulfenic, sulfinic or sulfonic acid), which destabilizes the toxin. The nuclear magnetic resonance structure of [C117S]YmoB and the homology model of TomB show that the two proteins form a four-helix bundle with a conserved buried cysteine connected to the exterior by a channel with a diameter comparable to that of an oxygen molecule. The Hha interaction site is located on the opposite side of the helix bundle.
Issue Date: 8-Dec-2016
Date of Acceptance: 18-Oct-2016
URI: http://hdl.handle.net/10044/1/61052
DOI: https://dx.doi.org/10.1038/ncomms13634
ISSN: 2041-1723
Publisher: Nature Publishing Group
Journal / Book Title: Nature Communications
Volume: 7
Copyright Statement: © 2016 The Author(s). This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Keywords: MD Multidisciplinary
Publication Status: Published
Article Number: 13634
Online Publication Date: 2016-12-08
Appears in Collections:Clinical Sciences
Molecular Sciences
Faculty of Medicine



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