Abstract
Glutathione S-transferases (GSTs) are involved in many stress responses in plants, for example, participating in the detoxification of xenobiotics and limiting oxidative damage. Studies examining the regulation of this gene family in diverse plant species have focused primarily on RNA expression. A proteomics method was developed to identify GSTs expressed in Arabidopsis seedlings and to determine how the abundance of these proteins changed in response to copper, a promoter of oxidative stress, and benoxacor, a herbicide safener. Eight GSTs were identified in seedlings grown under control conditions, and only one, AtGSTU19, was induced by benoxacor. In contrast, four GSTs, AtGSTF2, AtGSTF6, AtGSTF7, and AtGSTU19, were significantly more abundant in copper-treated seedlings. The different responses to these treatments may reflect the potential for copper to affect many more aspects of plant growth and physiology compared with a herbicide safener. Differences between RNA and protein expression of GSTs indicate that both transcriptional and translational mechanisms are involved in regulation of GSTs under these conditions.
Highlights
Glutathione S-transferases (GSTs)1 are a collection of multifunctional proteins that are found in essentially all organisms
One peptide (IQNGCSNVVSVDADSVVDGY) was identified that had a significant match to a protein other than an Arabidopsis GST. The function of this protein, encoded by gene At2g28540, is unknown and does not share significant sequence homology with any other characterized gene product. These results demonstrate that this technique can be used to identify GST proteins expressed in Arabidopsis seedlings and that GSH affinity chromatography provides an efficient method to reduce the complexity of protein samples, allowing for analysis focused on GSTs
RNA expression of genes encoding GSTs is influenced by diverse abiotic and biotic factors in plants and other organisms, but relatively little is known about the effects of these stimuli on expression of plant GST proteins
Summary
Glutathione S-transferases (GSTs)1 ( glutathione transferases) are a collection of multifunctional proteins that are found in essentially all organisms. A proteomics method was developed to identify GSTs expressed in Arabidopsis seedlings and to determine how the abundance of these proteins changed in response to copper, a promoter of oxidative stress, and benoxacor, a herbicide safener.
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