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, Miquel Pons

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12 Scopus citations

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 -SO x H-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.

Original languageEnglish (US)
Article number13634
JournalNature communications
Volume7
DOIs
StatePublished - Dec 8 2016

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

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    Marimon, O., Teixeira, J. M. C., Cordeiro, T. N., Soo, V. W. C., Wood, T. L., Mayzel, M., Amata, I., García, J., Morera, A., Gay, M., Vilaseca, M., Orekhov, V. Y., Wood, T. K., & Pons, M. (2016). An oxygen-sensitive toxin-antitoxin system. Nature communications, 7, [13634]. https://doi.org/10.1038/ncomms13634