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How have glutathione S-transferases evolved in plants? 

Monooxygenase
Medicine
Cytochrome P450
Lineage (genetic)
Plant protein
Best insight from top research papers

Glutathione S-transferases (GSTs) in plants have evolved through gene duplication and horizontal gene transfer. The evolution of GSTs in plants occurred before the divergence of land plants and streptophyte algae from their last common ancestor . Gene duplications in certain GST classes, such as Phi and Tau, led to the larger numbers of GST proteins found in land plants compared to algae . GSTs play a role in herbicide resistance, with alleles conferring resistance evolving in recent years in certain GST classes, including Phi and Tau . Additionally, GSTs have been found to be involved in multiple herbicide resistance (MHR) in weed populations, with enhanced metabolism and detoxifying ability of GSTs contributing to MHR . The structure and function of GSTs have been studied, and specific structural elements have been identified that are responsible for catalytic efficiency, thermal stability, and inhibition potency . Overall, the evolution of GSTs in plants involves gene duplication, horizontal gene transfer, and their role in herbicide resistance and MHR .

Answers from top 4 papers

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Papers (4)Insight
Open access•Posted Content•DOI
Fungi ligE-type glutathione S-transferases horizontally transferred into plants and a protozoan
Meng Zhang, Dan Li 
26 Jun 2020-bioRxiv
The paper mentions that ligE-type glutathione S-transferases (GSTs) have evolved in various fungi and are also found in some liverworts and green algae. However, it does not provide specific information on how GSTs have evolved in plants.
Open access•Journal Article•DOI
Glutathione S-transferase: a versatile protein family.
Swati Vaish, Divya Gupta, Rajesh Mehrotra, Sandhya Mehrotra, Mahesh K. Basantani 
27 Jun 2020
56 Citations
The paper provides information on the evolution of glutathione S-transferases (GSTs) in plants, including their distribution, structural features, and diverse roles in plant functions.
Open access•Journal Article•DOI
Genes encoding cytochrome P450 monooxygenases and glutathione S-transferases associated with herbicide resistance evolved before the origin of land plants
17 Feb 2023-PLOS ONE
The paper states that glutathione S-transferases (GSTs) are an ancient superfamily of enzymes found in plants. It also mentions that the number of GST genes encoded in the genomes of land plants is larger than in algae, suggesting that GSTs have evolved through gene expansions in land plants.
Open access•Posted Content•DOI
Genes encoding cytochrome P450 monooxygenases and glutathione S-transferases associated with herbicide resistance evolved before the origin of land plants
Alexandra Casey, Liam Dolan 
14 Aug 2022-bioRxiv
1 Citations
The paper states that glutathione S-transferases (GST) in plants evolved before the divergence of land plants and streptophyte algae from their last common ancestor. It also mentions that gene duplication in two of the fourteen GST classes led to the large numbers of GST proteins found in extant land plants. However, it does not provide specific details on how GSTs have evolved in plants.

Related Questions

What is the evolutionary history of glutathione S-transferases in plants?4 answersGlutathione S-transferases (GSTs) in plants have evolved through gene duplication and horizontal gene transfer events. The GST supergene family in plants is highly conserved and has been found to be conserved in evolution with the GST supergene family in Arabidopsis. The GST supergene family in Euphorbiaceae plants, a family known for its economic importance, has been classified into 10 subfamilies based on sequence characteristics and conserved domain types. These GSTs play a role in detoxification, oxidative stress response, growth and development, and herbicide detoxification in plants. The evolution of GSTs in plants involves gene amplification through tandem repeats and translocations, as well as strong purification selection. Furthermore, GSTs have been found to have diverse roles in plant functions, including secondary metabolism and response to biotic and abiotic stresses. Overall, the evolutionary history of GSTs in plants involves gene duplication, horizontal gene transfer, and conservation of function across different plant species.
What is the significance of glutathione metabolism in plant ?4 answersStep 1: Glutathione metabolism in plants is significant for maintaining redox homeostasis, protecting against oxidative stress, and detoxifying xenobiotics and toxic compounds. It also plays a crucial role in plant growth, development, and response to changing environments. Glutathione acts as a non-enzymatic antioxidant, regulates metabolic functions, and is involved in the detoxification of cytotoxic molecules and toxic metals. Additionally, it controls gene expression, cell cycle progression, and the synthesis of phytochelatins. The maintenance of a high GSH/GSSG ratio is essential for physiological functions and stress tolerance, making glutathione metabolism a key factor in plant adaptation to adverse environmental conditions. Step 3: Glutathione metabolism in plants is significant for maintaining redox homeostasis, protecting against oxidative stress, and detoxifying xenobiotics and toxic compounds. It also plays a crucial role in plant growth, development, and response to changing environments. Glutathione acts as a non-enzymatic antioxidant, regulates metabolic functions, and is involved in the detoxification of cytotoxic molecules and toxic metals. Additionally, it controls gene expression, cell cycle progression, and the synthesis of phytochelatins. The maintenance of a high GSH/GSSG ratio is essential for physiological functions and stress tolerance, making glutathione metabolism a key factor in plant adaptation to adverse environmental conditions.
What is the definition of glutathione?5 answersGlutathione is a tripeptide composed of three amino acids: glutamate, cysteine, and glycine. It acts as an antioxidant, protecting cells against oxidative stress. Glutathione also has other important functions, such as detoxification, immune system modulation, and regulation of cellular proliferation and apoptosis. Decreased levels of glutathione have been associated with various diseases, including cancer, Alzheimer's disease, and Parkinson's disease. Glutathione is synthesized at the cytosolic level and exists in cells in a reduced form (thiol-reduced-GSH-) and an oxidized form (disulfide-oxidized). It plays a therapeutic role in chronic diseases characterized by altered redox balance and reduced GSH levels, such as neurodegenerative disorders, cancer, and chronic liver diseases. Glutathione is a naturally occurring compound that plays a crucial role in the cellular response to oxidative stress. It can be used as a potential marker for human diseases, and both natural and synthetic glutathione can be used to replenish its pool.
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