A key metabolic integrator, coenzyme A, modulates the activity of peroxiredoxin 5 via covalent modification

Molecular and Cellular Biochemistry
Jovana BakovićIvan Gout

Abstract

Peroxiredoxins (Prdxs) are antioxidant enzymes that catalyse the breakdown of peroxides and regulate redox activity in the cell. Peroxiredoxin 5 (Prdx5) is a unique member of Prdxs, which displays a wider subcellular distribution and substrate specificity and exhibits a different catalytic mechanism when compared to other members of the family. Here, the role of a key metabolic integrator coenzyme A (CoA) in modulating the activity of Prdx5 was investigated. We report for the first time a novel mode of Prdx5 regulation mediated via covalent and reversible attachment of CoA (CoAlation) in cellular response to oxidative and metabolic stress. The site of CoAlation in endogenous Prdx5 was mapped by mass spectrometry to peroxidatic cysteine 48. By employing an in vitro CoAlation assay, we showed that Prdx5 peroxidase activity is inhibited by covalent interaction with CoA in a dithiothreitol-sensitive manner. Collectively, these results reveal that human Prdx5 is a substrate for CoAlation in vitro and in vivo, and provide new insight into metabolic control of redox status in mammalian cells.

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Citations

Dec 3, 2020·International Journal of Molecular Sciences·Aleksandra CzumajEwa Stelmanska
Jan 28, 2021·International Journal of Molecular Sciences·Jovana BakovićIvan Gout
Feb 12, 2021·Expert Opinion on Therapeutic Patents·Chirag C Mehta, Hardik G Bhatt

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Methods Mentioned

BETA
acetylation
transfection
immunoprecipitation
Protein Assay
affinity purification
pull-down
pull-downs
pulled down

Software Mentioned

Image Studio Lite
Andromeda
MaxQuant

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