Glutathione Metabolism in Plants under Stress: Beyond Reactive Oxygen Species Detoxification

Glutathione is an essential metabolite for plant life best known for its role in the control of reactive oxygen species (ROS). Glutathione is also involved in the detoxification of methylglyoxal (MG) which, much like ROS, is produced at low levels by aerobic metabolism under normal conditions. While...

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Vydáno v:Metabolites Ročník 11; číslo 9; s. 641
Hlavní autoři: Dorion, Sonia, Ouellet, Jasmine C., Rivoal, Jean
Médium: Journal Article
Jazyk:angličtina
Vydáno: Basel MDPI AG 19.09.2021
MDPI
Témata:
Abiotic stress
Alternative splicing
Biosynthesis
Carbohydrates
Detoxification
Enzymes
Fatty acids
Glutathione
glyoxalase pathway
Isoforms
Metabolism
Metabolites
Oxidation
Oxidative stress
Phosphates
Photosynthesis
plant stress
Post-translation
Proteins
Pyruvaldehyde
Reactive oxygen species
Respiration
Review
S-glutathionylation
ISSN:2218-1989, 2218-1989
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Shrnutí:Glutathione is an essential metabolite for plant life best known for its role in the control of reactive oxygen species (ROS). Glutathione is also involved in the detoxification of methylglyoxal (MG) which, much like ROS, is produced at low levels by aerobic metabolism under normal conditions. While several physiological processes depend on ROS and MG, a variety of stresses can dramatically increase their concentration leading to potentially deleterious effects. In this review, we examine the structure and the stress regulation of the pathways involved in glutathione synthesis and degradation. We provide a synthesis of the current knowledge on the glutathione-dependent glyoxalase pathway responsible for MG detoxification. We present recent developments on the organization of the glyoxalase pathway in which alternative splicing generate a number of isoforms targeted to various subcellular compartments. Stress regulation of enzymes involved in MG detoxification occurs at multiple levels. A growing number of studies show that oxidative stress promotes the covalent modification of proteins by glutathione. This post-translational modification is called S-glutathionylation. It affects the function of several target proteins and is relevant to stress adaptation. We address this regulatory function in an analysis of the enzymes and pathways targeted by S-glutathionylation.
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Co-first author, these authors contributed equally to this work.
ISSN:2218-1989
2218-1989
DOI:10.3390/metabo11090641