Plant glutathione transferases.
Plant glutathione transferases.
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DOI:
10.1186/gb-2002-3-3-reviews3004
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发表时间:
2002
期刊:
影响因子:
12.3
通讯作者:
Edwards R
中科院分区:
文献类型:
--
作者:
Dixon DP;Lapthorn A;Edwards R
The soluble glutathione transferases (GSTs) are a large, conserved family of proteins that use the tripeptide glutathione as a cosubstrate or coenzyme. They are predominantly expressed in the cytosol and have a range of catalytic and non-catalytic functions, including detoxification of herbicides and protection from oxidative stress, and have been implicated in other cellular processes. The 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.
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影响因子:
4.7
作者:
Cummins, I;Cole, DJ;Edwards, R
通讯作者:
Edwards, R
影响因子:
11.6
作者:
Loyall, L;Uchida, K;Frohnmeyer, H
通讯作者:
Frohnmeyer, H
DOI:
10.1016/s0969-2126(98)00074-4
发表时间:
1998-06-15
期刊:
STRUCTURE WITH FOLDING & DESIGN
影响因子:
--
作者:
Rossjohn, J;Polekhina, G;Parker, MW
通讯作者:
Parker, MW
影响因子:
6.4
作者:
Gonneau, J;Mornet, R;Laloue, M
通讯作者:
Laloue, M
影响因子:
1.9
作者:
SARIGORLA, M;FERRARIO, S;VILLA, M
通讯作者:
VILLA, M