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An oxygen-sensitive toxin–antitoxin system

Author

Listed:
  • 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
    Present address: X-ray and Neutron Science, Niels Bohr Institute, Copenhagen, 2100, Denmark)

  • 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
    Present address: CNRS FRE 3630 (affiliated with Univ. Paris Diderot, Sorbonne Paris Cité), Institut de Biologie Physico-Chimique, Paris 75006, France)

  • Jesús García

    (Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona
    Institute for Research in Biomedicine (IRB-Barcelona), The Barcelona Institute of Science and Technology)

  • Ainara Morera

    (Biomolecular NMR Laboratory, Organic Chemistry Section, University of Barcelona
    Present address: Departament de Física Fonamental, Martí i Franquès, Barcelona 1-11 08028, Spain)

  • 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)

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.

Suggested Citation

  • 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, 2016. "An oxygen-sensitive toxin–antitoxin system," Nature Communications, Nature, vol. 7(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13634
    DOI: 10.1038/ncomms13634
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