TGA2 signaling in response to reactive electrophile species is not dependent on cysteine modification of TGA2

Simone Findling, Henrik U. Stotz, Maria Zoeller, Markus Krischke, Mark Zander, Christiane Gatz, Susanne Berger, Martin J. Mueller

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Reactive electrophile species (RES), including prostaglandins, phytoprostanes and 12-oxo phytodienoic acid (OPDA), activate detoxification responses in plants and animals. However, the pathways leading to the activation of defense reactions related to abiotic or biotic stress as a function of RES formation, accumulation or treatment are poorly understood in plants. Here, the thiol-modification of proteins, including the RES-activated basic region/leucine zipper transcription factor TGA2, was studied. TGA2 contains a single cysteine residue (Cys186) that was covalently modified by reactive cyclopentenones but not required for induction of detoxification genes in response to OPDA or prostaglandin A1. Activation of the glutathione-S-transferase 6 (GST6) promoter was responsive to cyclopentenones but not to unreactive cyclopentanones, including jasmonic acid suggesting that thiol reactivity of RES is important to activate the TGA2-dependent signaling pathway resulting in GST6 activation We show that RES modify thiols in numerous proteins in vivo, however, thiol reactivity alone appears not to be sufficient for biological activity as demonstrated by the failure of several membrane permeable thiol reactive reagents to activate the GST6 promoter.

Original languageEnglish (US)
Article numbere0195398
JournalPloS one
Volume13
Issue number4
DOIs
StatePublished - Apr 2018
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

Fingerprint

Dive into the research topics of 'TGA2 signaling in response to reactive electrophile species is not dependent on cysteine modification of TGA2'. Together they form a unique fingerprint.

Cite this