ArticleJournal of experimental botany2009
Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily.
Article in Journal of experimental botany, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
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Who cites it
122 citing papers in PubMed, 305 citations in OpenAlex.
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- Hydrogen peroxide, ascorbate, and glutathione: building the Foyer-Halliwell-Asada pathway.Planta · 2025Review
- Genome-wide identification and in silico analysis of GSTs reveals hormone mediated stress response in saffron.Frontiers in plant science · 2025Article
- Overlooked and misunderstood: can glutathione conjugates be clues to understanding plant glutathione transferases?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
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- Genome-wide transcriptional profiling provides clues to molecular mechanisms underlying cold tolerance in chickpea.Scientific reports · 2023Article
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- Organelles and phytohormones: a network of interactions in plant stress responses.Journal of experimental botany · 2022Review
- AtGSTU19 and AtGSTU24 as Moderators of the Response ofInternational journal of molecular sciences · 2022Article
- Transcriptional response of a target plant to benzoxazinoid and diterpene allelochemicals highlights commonalities in detoxification.BMC plant biology · 2022Article
- Genome-Wide Identification of Glutathione S-Transferase and Expression Analysis in Response to Anthocyanin Transport in the Flesh of the New Teinturier Grape Germplasm 'Zhongshan-HongYu'.International journal of molecular sciences · 2022Article
- Phytoremediation of uranium-contaminated soil by perennial ryegrass (Lolium perenne L.) enhanced with citric acid application.Environmental science and pollution research international · 2022Article
- Transcriptome profiling of Arabidopsis thaliana roots in response to allelopathic effects of Conyza canadensis.Ecotoxicology (London, England) · 2022Article
62 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Enzyme screens with Strep-tagged recombinant proteins and expression studies with the respective green fluorescent protein (GFP) fusions have been employed to examine the functional activities and subcellular localization of members of the Arabidopsis glutathione transferase (GST) superfamily. Fifty-one of 54 GST family members were transcribed and 41 found to express as functional glutathione-dependent enzymes in Escherichia coli. Functional redundancy was observed and in particular three theta (T) class GSTs showed conserved activities as hydroperoxide-reducing glutathione peroxidases (GPOXs). When expressed in tobacco as GFP fusions, all three GSTTs localized to the peroxisome, where their GPOX activity could prevent membrane damage arising from fatty acid oxidation. Through alternative splicing, two of these GSTTs form fusions with Myb transcription factor-like domains. Examination of one of these variants showed discrete localization within the nucleus, possibly serving a role in reducing nucleic acid hydroperoxides or in signalling. Based on this unexpected differential sub-cellular localization, 15 other GST family members were expressed as GFP fusions in tobacco. Most accumulated in the cytosol, but GSTU12 localized to the nucleus, a family member resembling a bacterial tetrachlorohydroquinone dehalogenase selectively associated with the plasma membrane, and a lambda GSTL2 was partially directed to the peroxisome after removal of a putative chloroplast transit peptide. Based on the results obtained with the GSTTs, it was concluded that these proteins can exert identical protective functions in differing subcellular compartments.
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