ArticlePloS one2020
Zn2+ dependent glyoxalase I plays the major role in methylglyoxal detoxification and salinity stress tolerance in plants.
Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- ABI4-HDA9 Module Epigenetically Silences GIG1 to Accumulate Methylglyoxal for Seed Thermoinhibition Response in Arabidopsis thaliana.Plant, cell & environment · 2026Article
- AtGLYI3 and AtGLYI6 play the major role in nickel stress tolerance in Arabidopsis thaliana.Plant cell reports · 2026Article
- Role of methylglyoxal and glyoxalase in the regulation of plant response to heavy metal stress.Plant cell reports · 2024Review
- Article
- Identification of new potential molecular actors related to fiber quality in flax through Omics.Frontiers in plant science · 2023Article
- Glyoxalase I activity affects Arabidopsis sensitivity to ammonium nutrition.Plant cell reports · 2022Article
- Glutathione Metabolism in Plants under Stress: Beyond Reactive Oxygen Species Detoxification.Metabolites · 2021Review
- The metabolite methylglyoxal-mediated gene expression is associated with histone methylglyoxalation.Nucleic acids research · 2021Article
- Functional characterization of the Glyoxalase-I (Plant signaling & behavior · 2020Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glyoxalase pathway is the major pathway of methylglyoxal detoxification and is ubiquitously present in all organisms ranging from prokaryotes to eukaryotes. Glyoxalase I (GLYI) and Glyoxalase II (GLYII), the two core enzymes of this pathway work together to neutralize methylglyoxal (MG), a dicarbonyl molecule with detrimental cytotoxicity at higher concentrations. The first step towards the detoxification of MG is catalyzed by GLYI, a metalloenzyme that requires divalent metal ions (either Zn2+ as seen in eukaryotes or Ni2+ as in prokaryotes). However, both Zn2+ and Ni2+ dependent GLYIs have been shown to co-exist in a higher eukaryote i.e. Arabidopsis thaliana. In the present study, we determine the role of both Zn2+ dependent (AtGLYI2) and Ni2+ dependent (AtGLYI3, AtGLYI6) GLYIs from Arabidopsis in salinity stress tolerance. AtGLYI2 overexpressing Arabidopsis plants showed better growth rate while maintaining lower levels of MG under high saline conditions. They were taller with more number of silique formation with respect to their Ni2+ dependent counterparts. Further, lack in germination of Arabidopsis AtGLYI2 mutants in presence of exogenous MG indicates the direct involvement of Zn2+ dependent GLYI in MG detoxification, suggesting Zn2+ dependent GLYI as the main enzyme responsible for MG detoxification and salinity stress tolerance.
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