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Profiling of advanced glycation end products uncovers abiotic stress-specific target proteins in Arabidopsis

Chaplin, Amanda K and Chernukhin, Igor and Bechtold, Ulrike (2019) 'Profiling of advanced glycation end products uncovers abiotic stress-specific target proteins in Arabidopsis.' Journal of Experimental Botany, 70 (2). 653 - 670. ISSN 0022-0957

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Abstract

Non-enzymatic post-translational modifications of proteins can occur when the nucleophilic amino acid side chains of lysine and arginine encounter a reactive metabolite to form advanced glycation end products (AGEs). Glycation arises predominantly from the degradation of reducing sugars, and glycation has been observed during metabolic stress from glucose metabolism in both animals and plants. The implications of glycating proteins on plant proteins and biology has received little attention, and here we describe a robust assessment of global glycation profiles. We identified 112 glycated proteins that were common under a range of growth conditions and abiotic stress treatments, but also showed rosette age, diurnal, and drought stress-specific targets. Among 18 drought stress-specific glycation targets included several thioredoxin and thioredoxin-like proteins. In vitro glycation of two carbohydrate metabolism enzymes led either to a reduction or to a complete inhibition of activity, demonstrating the impact of glycation on protein function. Taken together, our results suggest that stress-specific glycation patterns of a small number of regulatory proteins may have a much broader impact on downstream target proteins that are, for example, associated with primary metabolism.

Item Type: Article
Uncontrolled Keywords: Abiotic stress, advanced glycation end products (AGEs), chloroplast, diurnal, drought, photosynthesis, protein glycation
Subjects: Q Science > QK Botany
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Elements
Date Deposited: 25 Feb 2019 11:48
Last Modified: 25 Feb 2019 11:48
URI: http://repository.essex.ac.uk/id/eprint/24102

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