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Title: An oxygen-sensitive toxin-antitoxin system
Author: Marimon Garrido, Oriol
Teixeira, J.M.C.
Cordeiro, Tiago N.
Soo, Valerie W. C.
Wood, Thammajun L.
Mayzel, Maxim
Amata, Irene
Gracía, Jesús
Morera, Ainara
Gay i Marín, Marina
Vilaseca Casas, Marta
Orekhov, V. Yu.
Wood, Thomas K.
Pons Vallès, Miquel
Keywords: Espectrometria de masses
Espectroscòpia de ressonància magnètica nuclear
Escheríchia coli
Mass spectrometry
Nuclear magnetic resonance spectroscopy
Escherichia coli
Issue Date: 8-Dec-2016
Publisher: Nature Publishing Group
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.
Note: Reproducció del document publicat a:
It is part of: Nature Communications, 2016, vol. 7, num. 13634
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ISSN: 2041-1723
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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