Protein redox regulation in the thylakoid lumen: the importance of disulfide bonds for violaxanthin de-epoxidase

FEBS Letters
Diana SimionatoTomas Morosinotto

Abstract

When exposed to saturating light conditions photosynthetic eukaryotes activate the xanthophyll cycle where the carotenoid violaxanthin is converted into zeaxanthin by the enzyme violaxanthin de-epoxidase (VDE). VDE protein sequence includes 13 cysteine residues, 12 of which are strongly conserved in both land plants and algae. Site directed mutagenesis of Arabidopsis thaliana VDE showed that all these 12 conserved cysteines have a major role in protein function and their mutation leads to a strong reduction of activity. VDE is also shown to be active in its completely oxidized form presenting six disulfide bonds. Redox titration showed that VDE activity is sensitive to variation in redox potential, suggesting the possibility that dithiol/disulfide exchange reactions may represent a mechanism for VDE regulation.

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Citations

Jan 27, 2016·Journal of Plant Physiology·Zhen-Hui Kang, Gui-Xue Wang
Apr 30, 2016·Annual Review of Plant Biology·Bob B Buchanan
Feb 13, 2016·Physiologia Plantarum·Erik Ingmar HallinHans-Erik Åkerlund
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Jan 29, 2020·Antioxidants & Redox Signaling·Juanjuan YuShaojun Dai
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Jul 31, 2019·International Journal of Molecular Sciences·Xingji PengHonghui Lin
May 20, 2020·Frontiers in Plant Science·Reimund Goss, Dariusz Latowski
Nov 30, 2019·Plant Science : an International Journal of Experimental Plant Biology·Tianhu Sun, Li Li
Jun 19, 2021·Scientific Reports·Lander BlommaertBenjamin Bailleul
Jul 22, 2021·The Plant Journal : for Cell and Molecular Biology·Antonio J SerratoMariam Sahrawy

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