Publication details for Prof Robert EdwardsDixon, D.P., Lapthorn, A. & Edwards, R. (2002). Plant glutathione transferases. Genome Biology 3: reviews3004.1-3004.10.
- Publication type: Journal papers: academic
- ISSN/ISBN: 1465-6906, 1465-6914
- DOI: 10.1186/gb-2002-3-3-reviews3004
- View online: Online version
- Durham research online: DRO record
Author(s) from Durham
- Prof Robert Edwards
- Dr David P. Dixon
The soluble glutathione transferases (GSTs, EC 188.8.131.52) 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.