ArticlePloS one2016
Arabidopsis thaliana Contains Both Ni2+ and Zn2+ Dependent Glyoxalase I Enzymes and Ectopic Expression of the Latter Contributes More towards Abiotic Stress Tolerance in E. coli.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Mapping the Molecular Evolution and Role of Wild Rice GLYIII Protein-Encoding Genes in Abiotic Stress Response.Biochemical genetics · 2026Article
- AtGLYI3 and AtGLYI6 play the major role in nickel stress tolerance in Arabidopsis thaliana.Plant cell reports · 2026Article
- Tracing the intraspecies expansion of glyoxalase genes and their expanding roles across the genus Oryza.Functional & integrative genomics · 2024Article
- Genomic identification, characterization, and stress-induced expression profiling of glyoxalase and D-lactate dehydrogenase gene families in Capsicum annuum.BMC plant biology · 2024Article
- Genome-Wide Analysis and Expression Profiling of Glyoxalase Gene Families Under Abiotic Stresses in Cucumber (International journal of molecular sciences · 2024Article
- Role of methylglyoxal and glyoxalase in the regulation of plant response to heavy metal stress.Plant cell reports · 2024Review
- Genome-Wide Identification and Functional Characterization of Stress Related Glyoxalase Genes inInternational journal of molecular sciences · 2023Article
- Glutathione Metabolism in Plants under Stress: Beyond Reactive Oxygen Species Detoxification.Metabolites · 2021Review
- Expression of Brassica napus GLO1 is sufficient to breakdown artificial self-incompatibility in Arabidopsis thaliana.Plant reproduction · 2020Article
- Functional characterization of the Glyoxalase-I (Plant signaling & behavior · 2020Article
- The Glyoxalase System-New Insights into an Ancient Metabolism.Antioxidants (Basel, Switzerland) · 2020Review
- A D-lactate dehydrogenase from rice is involved in conferring tolerance to multiple abiotic stresses by maintaining cellular homeostasis.Scientific reports · 2020Article
- Protein Glycation in Plants-An Under-Researched Field with Much Still to Discover.International journal of molecular sciences · 2020Review
- From methylglyoxal to pyruvate: a genome-wide study for the identification of glyoxalases and D-lactate dehydrogenases in Sorghum bicolor.BMC genomics · 2020Article
- Zn2+ dependent glyoxalase I plays the major role in methylglyoxal detoxification and salinity stress tolerance in plants.PloS one · 2020Article
- Genome-wide analysis of glyoxalase-like gene families in grape (Vitis vinifera L.) and their expression profiling in response to downy mildew infection.BMC genomics · 2019Article
- GLYI and D-LDH play key role in methylglyoxal detoxification and abiotic stress tolerance.Scientific reports · 2018Article
- Genome-wide dissection and expression profiling of unique glyoxalase III genes in soybean reveal the differential pattern of transcriptional regulation.Scientific reports · 2018Article
- Dissecting the Physiological Function of Plant Glyoxalase I and Glyoxalase I-Like Proteins.Frontiers in plant science · 2018Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glyoxalase pathway is ubiquitously found in all the organisms ranging from prokaryotes to eukaryotes. It acts as a major pathway for detoxification of methylglyoxal (MG), which deleteriously affects the biological system in stress conditions. The first important enzyme of this system is Glyoxalase I (GLYI). It is a metalloenzyme which requires divalent metal ions for its activity. This divalent metal ion can be either Zn2+ as found in most of eukaryotes or Ni2+ as seen in prokaryotes. In the present study, we have found three active GLYI enzymes (AtGLYI2, AtGLYI3 and AtGLYI6) belonging to different metal activation classes coexisting in Arabidopsis thaliana. These enzymes have been found to efficiently complement the GLYI yeast mutants. These three enzymes have been characterized in terms of their activity, metal dependency, kinetic parameters and their role in conferring tolerance to multiple abiotic stresses in E. coli and yeast. AtGLYI2 was found to be Zn2+ dependent whereas AtGLYI3 and AtGLYI6 were Ni2+ dependent. Enzyme activity of Zn2+ dependent enzyme, AtGLYI2, was observed to be exceptionally high (~250-670 fold) as compared to Ni2+ dependent enzymes, AtGLYI3 and AtGLYI6. The activity of these GLYI enzymes correlated well to their role in stress tolerance. Heterologous expression of these enzymes in E. coli led to better tolerance against various stress conditions. This is the first report of a higher eukaryotic species having multiple active GLYI enzymes belonging to different metal activation classes.
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