Plant glutathione transferases

By D. Dixon, A. Lapthorn, R. Edwards. Genome Biology, 2002

886 citations recorded by the source corpus.

SummaryThe soluble glutathione transferases (GSTs, EC 2.5.1.18) are encoded by a large and diverse gene family in plants, which can be divided on the basis of sequence identity into the phi, tau, theta, zeta and lambda classes. The theta and zeta GSTs have counterparts in animals but the other classes are plant-specific and form the focus of this article. The genome of Arabidopsis thaliana contains 48 GST genes, with the tau and phi classes being the most numerous. The GST proteins have evolved by gene duplication to perform a range of functional roles using the tripeptide glutathione (GSH) as a cosubstrate or coenzyme. GSTs are predominantly expressed in the cytosol, where their GSH-dependent catalytic functions include the conjugation and resulting detoxification of herbicides, the reduction of organic hydroperoxides formed during oxidative stress and the isomerization of maleylacetoacetate to fumarylacetoacetate, a key step in the catabolism of tyrosine. GSTs also have non-catalytic roles, binding flavonoid natural products in the cytosol prior to their deposition in the vacuole. Recent studies have also implicated GSTs as components of ultraviolet-inducible cell signaling pathways and as potential regulators of apoptosis. Although sequence diversification has produced GSTs with multiple functions, the structure of these proteins has been highly conserved. The GSTs thus represent an excellent example of how protein families can diversify to fulfill multiple functions while conserving form and structure.

Subfields: Molecular Biology, Nutrition and Dietetics

View Paper: https://www.semanticscholar.org/paper/e65f9d6ef911ca22b8be070d1d6ca367aabba4a4

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Sudesh Kumar Yadav
2. R. Edwards
3. D. Dixon
4. Naser Anjum
5. D. E. Rao
6. N. Khan
7. M. Arshad
8. M. Prasad

In Nutrition and Dietetics

1. R. Edwards
2. D. Dixon
3. M. Prasad
4. M. Iqbal
5. Sudesh Kumar Yadav
6. Altaf Ahmad

Citations in the corpus

• Photosynthesis and antioxidative defense mechanisms in deciphering drought stress tolerance of crop plants (2016, background): “…is associated with the storage and transport of reduced sulphur (Kopriva et al. 2004), detoxification of xenobiotics via glutathione-S-transferase (Dixon et al. 2002), synthesis of phytochelatins, and in the regulation of redox homeostasis of the cell together with its oxidised form (GSSG)…”
• Root-to-shoot Cd translocation via the xylem is the major process determining shoot and grain cadmium accumulation in rice (2009, positive): “2) thioltransferases or reductases (DHARs and GSTLs) (Dixon et al., 2002a) or isomerases (GSTZs) (Dixon and Edwards, 2006).”
• Glutathione Transferases (2010, methodology): “Thus, gel fi ltration experiments showed that DHAR1 and DHAR3 both eluted with a retention time consistent with being monomers (Dixon et al., 2002b), though this unusual behaviour has not yet been validated by other techniques.”
• Heavy metals toxicity in plants: An overview on the role of glutathione and phytochelatins in heavy metal stress tolerance of plants (2010, background): “The conjugation of GSH with such molecules is governed by glutathione Stransferase (Edwards et al., 2000; Edwards and Dixon, 2005).”
• Plant glutathione transferases — a decade falls short (2007, background): “Some of the structural characteristics of GSTs are also observed in other GSH-dependent proteins, such as glutaredoxin (Dixon et al. 2002b).”
• Carotenoid oxidation products are stress signals that mediate gene responses to singlet oxygen in plants (2012, background): “By catalyzing the conjugation of glutathione or sugar with a variety of substrates, GSTs and glycosyltransferases can detoxify compounds (37, 38).”
• Bioremediation and Phytoremediation of Pesticides: Recent Advances (2009, background): “In most cases, glutathione (GSH) forms conjugates with various xenobiotics such as pesticides by nucleophilic addition reactions catalyzed by glutathione-S-transferase (GST) (Dietz & Schnoor, 2001; Dixon et al., 2002; Edwards et al., 2000).”