An oxygen-sensitive toxin–antitoxin system

Oriol Marimon, João M. C. Teixeira, Tiago N. Cordeiro, Valerie W. C. Soo, Thammajun L. Wood, Maxim Mayzel, Irene Amata, Jesús García, Ainara Morera, Marina Gay, Marta Vilaseca, Vladislav Yu Orekhov, Thomas K. Wood () and Miquel Pons ()
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Oriol Marimon: Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona
João M. C. Teixeira: Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona
Tiago N. Cordeiro: Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona
Valerie W. C. Soo: Pennsylvania State University
Thammajun L. Wood: Pennsylvania State University
Maxim Mayzel: Swedish NMR Centre, Gothenburg University
Irene Amata: Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona
Jesús García: Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona
Ainara Morera: Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona
Marina Gay: Institute for Research in Biomedicine (IRB-Barcelona), The Barcelona Institute of Science and Technology
Marta Vilaseca: Institute for Research in Biomedicine (IRB-Barcelona), The Barcelona Institute of Science and Technology
Vladislav Yu Orekhov: Swedish NMR Centre, Gothenburg University
Thomas K. Wood: Pennsylvania State University
Miquel Pons: Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms13634

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