期刊
NATURE COMMUNICATIONS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms13634
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资金
- Spanish MINECO [BIO2010-15683, BIO2013-45793R]
- European Structural Funds, FEDER
- EC FP7 BioNMR project [261863]
- ARO [W911NF-14-1-0279]
- MINECO (Government of Spain)
- NIGMS [P41-GM103311]
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)Hcontaining 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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