Dehydroascorbate Reductases and Glutathione Set a Threshold for High-Light–Induced Ascorbate Accumulation. Issue 1 (23rd March 2020)
- Record Type:
- Journal Article
- Title:
- Dehydroascorbate Reductases and Glutathione Set a Threshold for High-Light–Induced Ascorbate Accumulation. Issue 1 (23rd March 2020)
- Main Title:
- Dehydroascorbate Reductases and Glutathione Set a Threshold for High-Light–Induced Ascorbate Accumulation
- Authors:
- Terai, Yusuke
Ueno, Hiromi
Ogawa, Takahisa
Sawa, Yoshihiro
Miyagi, Atsuko
Kawai-Yamada, Maki
Ishikawa, Takahiro
Maruta, Takanori - Abstract:
- Abstract : Cooperation of dehydroascorbate reductases and glutathione sets a threshold for ascorbate accumulation under high-light stress in Arabidopsis. Abstract: Plants require a high concentration of ascorbate as a redox buffer for survival under stress conditions, such as high light. Dehydroascorbate reductases (DHARs) are enzymes that catalyze the reduction of DHA to ascorbate using reduced glutathione (GSH) as an electron donor, allowing rapid ascorbate recycling. However, a recent study using an Arabidopsis ( Arabidopsis thaliana ) triple mutant lacking all three DHAR genes (herein called ∆ dhar ) did not find evidence for their role in ascorbate recycling under oxidative stress. To further study the function of DHARs, we generated ∆ dhar Arabidopsis plants as well as a quadruple mutant line combining ∆ dhar with an additional vtc2 mutation that causes ascorbate deficiency. Measurements of ascorbate in these mutants under low- or high-light conditions indicated that DHARs have a nonnegligible impact on full ascorbate accumulation under high light, but that they are dispensable when ascorbate concentrations are low to moderate. Because GSH itself can reduce DHA nonenzymatically, we used the pad2 mutant that contains ∼30% of the wild-type GSH level. The pad2 mutant accumulated ascorbate at a wild-type level under high light; however, when the pad2 mutation was combined with ∆ dhar, there was near-complete inhibition of high-light–dependent ascorbate accumulation. TheAbstract : Cooperation of dehydroascorbate reductases and glutathione sets a threshold for ascorbate accumulation under high-light stress in Arabidopsis. Abstract: Plants require a high concentration of ascorbate as a redox buffer for survival under stress conditions, such as high light. Dehydroascorbate reductases (DHARs) are enzymes that catalyze the reduction of DHA to ascorbate using reduced glutathione (GSH) as an electron donor, allowing rapid ascorbate recycling. However, a recent study using an Arabidopsis ( Arabidopsis thaliana ) triple mutant lacking all three DHAR genes (herein called ∆ dhar ) did not find evidence for their role in ascorbate recycling under oxidative stress. To further study the function of DHARs, we generated ∆ dhar Arabidopsis plants as well as a quadruple mutant line combining ∆ dhar with an additional vtc2 mutation that causes ascorbate deficiency. Measurements of ascorbate in these mutants under low- or high-light conditions indicated that DHARs have a nonnegligible impact on full ascorbate accumulation under high light, but that they are dispensable when ascorbate concentrations are low to moderate. Because GSH itself can reduce DHA nonenzymatically, we used the pad2 mutant that contains ∼30% of the wild-type GSH level. The pad2 mutant accumulated ascorbate at a wild-type level under high light; however, when the pad2 mutation was combined with ∆ dhar, there was near-complete inhibition of high-light–dependent ascorbate accumulation. The lack of ascorbate accumulation was consistent with a marked increase in the ascorbate degradation product threonate. These findings indicate that ascorbate recycling capacity is limited in ∆ dhar pad2 plants, and that both DHAR activity and GSH content set a threshold for high-light–induced ascorbate accumulation. … (more)
- Is Part Of:
- Plant physiology. Volume 183:Issue 1(2020)
- Journal:
- Plant physiology
- Issue:
- Volume 183:Issue 1(2020)
- Issue Display:
- Volume 183, Issue 1 (2020)
- Year:
- 2020
- Volume:
- 183
- Issue:
- 1
- Issue Sort Value:
- 2020-0183-0001-0000
- Page Start:
- 112
- Page End:
- 122
- Publication Date:
- 2020-03-23
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.19.01556 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16199.xml