Study summary · research use only
The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coli
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This study, conducted in the bacterium Escherichia coli, used the genetically-encoded redox probe Grx1-roGFP2 to examine import of extracellular glutathione into the cytoplasm. The authors report that eliminating only two ATP-Binding Cassette (ABC) transporter systems, Gsi and Opp, abolished glutathione import in both its reduced (GSH) and oxidized (GSSG) forms. Removing Gsi alone prevented import of GSSG, while removing Opp alone substantially reduced uptake of GSH.
Abstract
Glutathione is the major thiol-based antioxidant in a wide variety of biological systems, ranging from bacteria to eukaryotes. As a redox couple, consisting of reduced glutathione (GSH) and its oxidized form, glutathione disulfide (GSSG), it is crucial for the maintenance of the cellular redox balance. Glutathione transport out of and into cellular compartments and the extracellular space is a determinant of the thiol-disulfide redox state of the organelles and bodily fluids in question, but is currently not well understood. Here we use the genetically-encoded, glutathione-measuring redox probe Grx1-roGFP2 to comprehensively elucidate the import of extracellular glutathione into the cytoplasm of the model organism Escherichia coli. The elimination of only two ATP-Binding Cassette (ABC) transporter systems, Gsi and Opp, completely abrogates glutathione import into E. coli's cytoplasm, both in its reduced and oxidized form. The lack of only one of them, Gsi, completely prevents import of GSSG, while the lack of the other, Opp, substantially retards the uptake of reduced glutathione (GSH).
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