The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coli
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 balan...
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| Language: | English |
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Elsevier
2025-02-01
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| Series: | Redox Biology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213231724004312 |
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| author | Lisa R. Knoke Maik Muskietorz Lena Kühn Lars I. Leichert |
| author_facet | Lisa R. Knoke Maik Muskietorz Lena Kühn Lars I. Leichert |
| author_sort | Lisa R. Knoke |
| collection | DOAJ |
| description | 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). |
| format | Article |
| id | doaj-art-ac55f8b95b154c33a6c2bdff894181b8 |
| institution | Kabale University |
| issn | 2213-2317 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Redox Biology |
| spelling | doaj-art-ac55f8b95b154c33a6c2bdff894181b82025-01-14T04:12:07ZengElsevierRedox Biology2213-23172025-02-0179103453The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coliLisa R. Knoke0Maik Muskietorz1Lena Kühn2Lars I. Leichert3Ruhr University Bochum, Institute for Biochemistry and Pathobiochemistry – Microbial Biochemistry, Bochum, GermanyRuhr University Bochum, Institute for Biochemistry and Pathobiochemistry – Microbial Biochemistry, Bochum, GermanyRuhr University Bochum, Institute for Biochemistry and Pathobiochemistry – Microbial Biochemistry, Bochum, GermanyCorresponding author.; Ruhr University Bochum, Institute for Biochemistry and Pathobiochemistry – Microbial Biochemistry, Bochum, GermanyGlutathione 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).http://www.sciencedirect.com/science/article/pii/S2213231724004312GlutathioneGlutathione transportABC transporterGsiOpp |
| spellingShingle | Lisa R. Knoke Maik Muskietorz Lena Kühn Lars I. Leichert The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coli Redox Biology Glutathione Glutathione transport ABC transporter Gsi Opp |
| title | The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coli |
| title_full | The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coli |
| title_fullStr | The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coli |
| title_full_unstemmed | The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coli |
| title_short | The ABC transporter Opp imports reduced glutathione, while Gsi imports glutathione disulfide in Escherichia coli |
| title_sort | abc transporter opp imports reduced glutathione while gsi imports glutathione disulfide in escherichia coli |
| topic | Glutathione Glutathione transport ABC transporter Gsi Opp |
| url | http://www.sciencedirect.com/science/article/pii/S2213231724004312 |
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