Function and Regulation of Chloroplast Peroxiredoxin IIE

• DOI: 10.3390/antiox10020152
• Publication Date: 2021-01-21T07:36:05Z
• Authors: Anna Dreyer; Patrick Treffon; Daniel Basiry; Anna Maria Jozefo...; Andrea Matros; Hans-Peter Mock; Karl-Josef Dietz
• Keywords: Peroxiredoxin; Post-translational regulation

Peroxiredoxins (PRX) are thiol peroxidases that highly conserved throughout all biological kingdoms. Increasing evidence suggests their high reactivity toward peroxides has a function not only in antioxidant defense but particular redox regulation of the cell. Peroxiredoxin IIE (PRX-IIE) is one three PRX types found plastids and previously been linked to pathogen protection from protein nitration. However, its posttranslational chloroplast network remained be explored. Using recombinant protein, it was shown peroxidatic Cys121 subjected multiple modifications, namely disulfide formation, S-nitrosation, S-glutathionylation, hyperoxidation. Slightly oxidized glutathione fostered S-glutathionylation inhibited activity vitro. Immobilized PRX-IIE allowed trapping subsequent identification interaction partners by mass spectrometry. Interaction with 14-3-3 υ confirmed vitro stimulated under oxidizing conditions. Interactions did depend on phosphorylation as revealed testing phospho-mimicry variants PRX-IIE. Based these data proposed 14-3-3υ guides PRX‑IIE certain target proteins, possibly for regulation. These findings together other identified potential type II PRXs localized plastids, mitochondria, cytosol provide new perspective regulatory