Please use this identifier to cite or link to this item:
http://hdl.handle.net/2445/107125
Title: | An oxygen-sensitive toxin-antitoxin system |
Author: | 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 |
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: https://doi.org/10.1038/ncomms13634 |
It is part of: | Nature Communications, 2016, vol. 7, num. 13634 |
URI: | http://hdl.handle.net/2445/107125 |
Related resource: | https://doi.org/10.1038/ncomms13634 |
ISSN: | 2041-1723 |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) Publicacions de projectes de recerca finançats per la UE |
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