Published in
Nature Research, Nature Communications, 1(7), 2016
DOI: 10.1038/ncomms13634
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An oxygen-sensitive toxin–antitoxin system
,
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 ,
Miquel Pons
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Abstract
AbstractThe 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.