Chloroplastic ascorbate peroxidases targeted to stroma or thylakoid membrane: The chicken or egg dilemma

Ascorbate peroxidases (APXs) are heme peroxidases that remove hydrogen peroxide in different subcellular compartments with concomitant ascorbate cycling. Here, we analysed and discussed phylogenetic and molecular features of the APX family. Ancient APX originated as a soluble stromal enzyme, and ear...

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Bibliographic Details
Published in:FEBS letters 2022-12, Vol.596 (23), p.2989-3004
Main Authors: Jardim‐Messeder, Douglas, Zamocky, Marcel, Sachetto‐Martins, Gilberto, Margis‐Pinheiro, Márcia
Format: Article
Language:English
Subjects:
alternative splicing
antioxidant metabolism
Antioxidants
Archaeplastida
ascorbate peroxidase
Ascorbate Peroxidases - genetics
Ascorbate Peroxidases - metabolism
chloroplasts
Chloroplasts - metabolism
gene duplication
Gene Expression Regulation, Plant
Hydrogen Peroxide - metabolism
mitochondria
neofunctionalization
Peroxidases - genetics
Peroxidases - metabolism
Phylogeny
reactive oxygen species
Thylakoids - metabolism
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Summary:Ascorbate peroxidases (APXs) are heme peroxidases that remove hydrogen peroxide in different subcellular compartments with concomitant ascorbate cycling. Here, we analysed and discussed phylogenetic and molecular features of the APX family. Ancient APX originated as a soluble stromal enzyme, and early during plant evolution, acquired both chloroplast‐targeting and mitochondrion‐targeting sequences and an alternative splicing mechanism whereby it could be expressed as a soluble or thylakoid membrane‐bound enzyme. Later, independent duplication and neofunctionalization events in some angiosperm groups resulted in individual genes encoding stromal, thylakoidal and mitochondrial isoforms. These data reaffirm the complexity of plant antioxidant defenses that allow diverse plant species to acquire new means to adapt to changing environmental conditions. Ancestral APX initially diverged as a soluble chloroplastidial enzyme (chlAPX). Duplication and neo‐functionalization events gave rise to isoforms with specific subcellular localization, including membrane‐bound chlAPX. In different angiosperm groups, individual evolutionary histories led to the emergence of chloroplastidial and mitochondrial APX, which have soluble and membrane‐bound isoforms generated through alternative splicing, from a dually targeted ancestor protein.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.14438