Plant dehydroascorbate reductase moonlights as membrane integrated ion channel
Copyright © 2023 Elsevier Inc. All rights reserved..
Plant dehydroascorbate reductases (DHARs) are only known as soluble antioxidant enzymes of the ascorbate-glutathione pathway. They recycle ascorbate from dehydroascorbate, thereby protecting plants from oxidative stress and the resulting cellular damage. DHARs share structural GST fold with human chloride intracellular channels (HsCLICs) which are dimorphic proteins that exists in soluble enzymatic and membrane integrated ion channel forms. While the soluble form of DHAR has been extensively studied, the existence of a membrane integrated form remains unknown. We demonstrate for the first time using biochemistry, immunofluorescence confocal microscopy, and bilayer electrophysiology that Pennisetum glaucum DHAR (PgDHAR) is dimorphic and is localized to the plant plasma membrane. In addition, membrane translocation increases under induced oxidative stress. Similarly, HsCLIC1 translocates more into peripheral blood mononuclear cells (PBMCs) plasma membrane under induced oxidative stress conditions. Moreover, purified soluble PgDHAR spontaneously inserts and conducts ions in reconstituted lipid bilayers, and the addition of detergent facilitates insertion. In addition to the well-known soluble enzymatic form, our data provides conclusive evidence that plant DHAR also exists in a novel membrane-integrated form. Thus, the structure of DHAR ion channel form will help gain deeper insights into its function across various life forms.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:741 |
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| Enthalten in: |
Archives of biochemistry and biophysics - 741(2023) vom: 13. Juni, Seite 109603 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Das, Bhaba Krishna [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 15.05.2023 Date Revised 25.05.2023 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.abb.2023.109603 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM355885603 |
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| 245 | 1 | 0 | |a Plant dehydroascorbate reductase moonlights as membrane integrated ion channel |
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| 520 | |a Copyright © 2023 Elsevier Inc. All rights reserved. | ||
| 520 | |a Plant dehydroascorbate reductases (DHARs) are only known as soluble antioxidant enzymes of the ascorbate-glutathione pathway. They recycle ascorbate from dehydroascorbate, thereby protecting plants from oxidative stress and the resulting cellular damage. DHARs share structural GST fold with human chloride intracellular channels (HsCLICs) which are dimorphic proteins that exists in soluble enzymatic and membrane integrated ion channel forms. While the soluble form of DHAR has been extensively studied, the existence of a membrane integrated form remains unknown. We demonstrate for the first time using biochemistry, immunofluorescence confocal microscopy, and bilayer electrophysiology that Pennisetum glaucum DHAR (PgDHAR) is dimorphic and is localized to the plant plasma membrane. In addition, membrane translocation increases under induced oxidative stress. Similarly, HsCLIC1 translocates more into peripheral blood mononuclear cells (PBMCs) plasma membrane under induced oxidative stress conditions. Moreover, purified soluble PgDHAR spontaneously inserts and conducts ions in reconstituted lipid bilayers, and the addition of detergent facilitates insertion. In addition to the well-known soluble enzymatic form, our data provides conclusive evidence that plant DHAR also exists in a novel membrane-integrated form. Thus, the structure of DHAR ion channel form will help gain deeper insights into its function across various life forms | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Chloride intracellular channel | |
| 650 | 4 | |a Dehydroascorbate reductase | |
| 650 | 4 | |a Dimorphic | |
| 650 | 4 | |a Ion channel | |
| 650 | 4 | |a Membrane protein | |
| 650 | 4 | |a Oxidative stress | |
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| 650 | 7 | |a Ascorbic Acid |2 NLM | |
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| 700 | 1 | |a Khan, Wajahat Ali |e verfasserin |4 aut | |
| 700 | 1 | |a Sreekumar, Sreeshma Nellootil |e verfasserin |4 aut | |
| 700 | 1 | |a Ponraj, Kannapiran |e verfasserin |4 aut | |
| 700 | 1 | |a Achary, V Mohan Murali |e verfasserin |4 aut | |
| 700 | 1 | |a Reddy, Elluri Seetharami |e verfasserin |4 aut | |
| 700 | 1 | |a Balasubramaniam, D |e verfasserin |4 aut | |
| 700 | 1 | |a Chandele, Anmol |e verfasserin |4 aut | |
| 700 | 1 | |a Reddy, Malireddy K |e verfasserin |4 aut | |
| 700 | 1 | |a Arockiasamy, Arulandu |e verfasserin |4 aut | |
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