Journal
METABOLITES
Volume 11, Issue 9, Pages -Publisher
MDPI
DOI: 10.3390/metabo11090641
Keywords
plant stress; glutathione; oxidative stress; glyoxalase pathway; S-glutathionylation; reactive oxygen species; methylglyoxal; metabolic adaptation
Categories
Funding
- Natural Sciences and Engineering Research Council of Canada [2019-05955]
- Fonds de Recherche du Quebec-Nature et Technologies
- Alexander-Graham-Bell Graduate Scholarship from the Natural Sciences and Engineering Research Council of Canada
Ask authors/readers for more resources
Glutathione plays a crucial role in plant life by controlling reactive oxygen species and detoxifying methylglyoxal. Oxidative stress can lead to covalent modification of proteins by glutathione, affecting their function and adaptation to stress.
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available