An Oxygen-Sensitive Toxin-Antitoxin System
Abstract
The Hha and TomB proteins from Escherichia coli form an oxygen-dependent toxinantitoxin (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.
Document Details
- Document Type
- Technical Report
- Publication Date
- Dec 08, 2016
- Accession Number
- AD1053491
Entities
People
- Ainara Morera
- Irene Amata
- Jesus Garcia
- Joao M. Teixeira
- Marina Gay
- Marta Vilaseca
- Maxim Mayzel
- Miquel Pons
- Oriol Marimon
- Thammajun L. Wood
- Thomas K. Wood
- Tiago N. Cordeiro
- Valerie W. Soo
- Vladislav Y. Orekhov