An oxygen-sensitive toxin-antitoxin system

Oriol Marimon, João M.C. Teixeira, Tiago N. Cordeiro, Valerie W.C. Soo, Thammajun Leungsakul Wood, Maxim Mayzel, Irene Amata, Jesús García, Ainara Morera, Marina Gay, Marta Vilaseca, Vladislav Yu Orekhov, Thomas Keith Wood, Miquel Pons

Research output: Contribution to journalArticle

10 Citations (Scopus)

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

Fingerprint

Antitoxins
cysteine
Cysteine
Oxygen
helices
bundles
oxygen
Sulfenic Acids
Sulfinic Acids
proteins
Yersinia
Sulfonic Acids
Escherichia coli Proteins
sulfonic acid
homology
Escherichia
Escherichia coli
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Oxidation

All Science Journal Classification (ASJC) codes

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

Cite this

Marimon, O., Teixeira, J. M. C., Cordeiro, T. N., Soo, V. W. C., Wood, T. L., Mayzel, M., ... Pons, M. (2016). An oxygen-sensitive toxin-antitoxin system. Nature communications, 7, [13634]. https://doi.org/10.1038/ncomms13634
Marimon, Oriol ; Teixeira, João M.C. ; Cordeiro, Tiago N. ; Soo, Valerie W.C. ; Wood, Thammajun Leungsakul ; Mayzel, Maxim ; Amata, Irene ; García, Jesús ; Morera, Ainara ; Gay, Marina ; Vilaseca, Marta ; Orekhov, Vladislav Yu ; Wood, Thomas Keith ; Pons, Miquel. / An oxygen-sensitive toxin-antitoxin system. In: Nature communications. 2016 ; Vol. 7.
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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 2016, 'An oxygen-sensitive toxin-antitoxin system', Nature communications, vol. 7, 13634. https://doi.org/10.1038/ncomms13634

An oxygen-sensitive toxin-antitoxin system. / Marimon, Oriol; Teixeira, João M.C.; Cordeiro, Tiago N.; Soo, Valerie W.C.; Wood, Thammajun Leungsakul; Mayzel, Maxim; Amata, Irene; García, Jesús; Morera, Ainara; Gay, Marina; Vilaseca, Marta; Orekhov, Vladislav Yu; Wood, Thomas Keith; Pons, Miquel.

In: Nature communications, Vol. 7, 13634, 08.12.2016.

Research output: Contribution to journalArticle

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AU - Marimon, Oriol

AU - Teixeira, João M.C.

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AU - Soo, Valerie W.C.

AU - Wood, Thammajun Leungsakul

AU - Mayzel, Maxim

AU - Amata, Irene

AU - García, Jesús

AU - Morera, Ainara

AU - Gay, Marina

AU - Vilaseca, Marta

AU - Orekhov, Vladislav Yu

AU - Wood, Thomas Keith

AU - Pons, Miquel

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N2 - 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.

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Marimon O, Teixeira JMC, Cordeiro TN, Soo VWC, Wood TL, Mayzel M et al. An oxygen-sensitive toxin-antitoxin system. Nature communications. 2016 Dec 8;7. 13634. https://doi.org/10.1038/ncomms13634