Files
Document type
ArticleVersion
Published versionPublication date
Publication license
Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/107125
An oxygen-sensitive toxin-antitoxin system
Journal Title
Director/Tutor
Journal ISSN
Volume Title
Related resource
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.
Subject (English)
Citation
Citation
MARIMON GARRIDO, Oriol, et al. An oxygen-sensitive toxin-antitoxin system. Nature Communications. 2016. Vol. 7, num. 13634. ISSN 2041-1723. [consulted: 13 of August of 2026]. Available at: https://hdl.handle.net/2445/107125