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Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/107125
An oxygen-sensitive toxin-antitoxin system
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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.
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MARIMON GARRIDO, Oriol, TEIXEIRA, Joao 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, Vladislav yu, WOOD, Thomas k., PONS VALLÈS, Miquel. An oxygen-sensitive toxin-antitoxin system. _Nature Communications_. 2016. Vol. 7, núm. 13634. [consulta: 14 de gener de 2026]. ISSN: 2041-1723. [Disponible a: https://hdl.handle.net/2445/107125]