An oxygen-sensitive toxin-antitoxin system

Oriol Marimon; João M.C. Teixeira; Tiago N. Cordeiro; Valerie W.C. Soo; Thammajun L. Wood; Maxim Mayzel; Irene Amata; Jesús García; Ainara Morera; Marina Gay; Marta Vilaseca; Vladislav Yu Orekhov; Thomas K. Wood; Miquel Pons

doi:10.1038/ncomms13634

An oxygen-sensitive toxin-antitoxin system

Oriol Marimon, João M.C. Teixeira, Tiago N. Cordeiro, Valerie W.C. Soo, Thammajun L. Wood, Maxim Mayzel, Irene Amata, Jesús García, Ainara Morera, Marina Gay, Marta Vilaseca, Vladislav Yu Orekhov, Thomas K. Wood, Miquel Pons

Research output: Contribution to journal › Article › peer-review

56 Scopus citations

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 -SO x H-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.

Original language	English (US)
Article number	13634
Journal	Nature communications
Volume	7
DOIs	https://doi.org/10.1038/ncomms13634
State	Published - Dec 8 2016

All Science Journal Classification (ASJC) codes

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy

Access to Document

10.1038/ncomms13634

Cite this

@article{c4244bd33ffe4b24a99313066d50a7a5,

title = "An oxygen-sensitive toxin-antitoxin system",

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 -SO x H-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.",

author = "Oriol Marimon and Teixeira, {Jo{\~a}o M.C.} and Cordeiro, {Tiago N.} and Soo, {Valerie W.C.} and Wood, {Thammajun L.} and Maxim Mayzel and Irene Amata and Jes{\'u}s Garc{\'i}a and Ainara Morera and Marina Gay and Marta Vilaseca and Orekhov, {Vladislav Yu} and Wood, {Thomas K.} and Miquel Pons",

note = "Publisher Copyright: {\textcopyright} The Author(s) 2016.",

year = "2016",

month = dec,

day = "8",

doi = "10.1038/ncomms13634",

language = "English (US)",

volume = "7",

journal = "Nature communications",

issn = "2041-1723",

publisher = "Nature Research",

}

TY - JOUR

T1 - An oxygen-sensitive toxin-antitoxin system

AU - Marimon, Oriol

AU - Teixeira, João M.C.

AU - Cordeiro, Tiago N.

AU - Soo, Valerie W.C.

AU - Wood, Thammajun L.

AU - Mayzel, Maxim

AU - Amata, Irene

AU - García, Jesús

AU - Morera, Ainara

AU - Gay, Marina

AU - Vilaseca, Marta

AU - Orekhov, Vladislav Yu

AU - Wood, Thomas K.

AU - Pons, Miquel

PY - 2016/12/8

Y1 - 2016/12/8

N2 - 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 H-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.

AB - 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 H-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.

UR - http://www.scopus.com/inward/record.url?scp=85005943302&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85005943302&partnerID=8YFLogxK

U2 - 10.1038/ncomms13634

DO - 10.1038/ncomms13634

M3 - Article

C2 - 27929062

AN - SCOPUS:85005943302

SN - 2041-1723

VL - 7

JO - Nature communications

JF - Nature communications

M1 - 13634

ER -

An oxygen-sensitive toxin-antitoxin system

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this