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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Veröffentlicht in:Metabolites Jg. 11; H. 9; S. 641
Hauptverfasser: Dorion, Sonia, Ouellet, Jasmine C., Rivoal, Jean
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Basel MDPI AG 19.09.2021
MDPI
Schlagworte:
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
Online-Zugang:Volltext
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Abstract 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.
AbstractList 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.
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.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.
Author Ouellet, Jasmine C.
Dorion, Sonia
Rivoal, Jean
AuthorAffiliation IRBV, Université de Montréal, 4101 rue Sherbrooke est, Montréal, QC H1X 2B2, Canada; sonia.dorion@umontreal.ca (S.D.); jasmine.ouellet@umontreal.ca (J.C.O.)
AuthorAffiliation_xml – name: IRBV, Université de Montréal, 4101 rue Sherbrooke est, Montréal, QC H1X 2B2, Canada; sonia.dorion@umontreal.ca (S.D.); jasmine.ouellet@umontreal.ca (J.C.O.)
Author_xml – sequence: 1
  givenname: Sonia
  surname: Dorion
  fullname: Dorion, Sonia
– sequence: 2
  givenname: Jasmine C.
  orcidid: 0000-0001-5016-2575
  surname: Ouellet
  fullname: Ouellet, Jasmine C.
– sequence: 3
  givenname: Jean
  surname: Rivoal
  fullname: Rivoal, Jean
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Snippet 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...
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StartPage 641
SubjectTerms 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
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Title Glutathione Metabolism in Plants under Stress: Beyond Reactive Oxygen Species Detoxification
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