Cysteine-mediated modulation of the glyoxalase system and HSP90 proteins enhances high-temperature stress tolerance in Arabidopsis thaliana

半胱氨酸介导的乙二醛酶系统和HSP90蛋白的调节增强了拟南芥的高温胁迫耐受性

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Abstract

High-temperature (HT) stress poses a major threat to plant growth and physiological functions by disrupting cellular homeostasis and metabolic processes. Despite extensive studies, the molecular and physiological mechanisms underlying plant adaptation to HT stress remain incompletely understood. This study investigates the role of cysteine (CYS), a thiol-containing amino acid, in enhancing high-temperature tolerance in Arabidopsis thaliana (A. thaliana) through the regulation of heat shock protein 90 (HSP90) and the glyoxalase (GLX) system. Our research demonstrates that CYS treatment under HT stress significantly enhances key physiological parameters, including relative water content (RWC), and total chlorophyll levels while reducing oxidative damage markers like thiobarbituric acid reactive substances (TBARS), and hydrogen peroxide (H₂O₂). In this study, findings from A. thaliana (Col-0, hsp90.1 and hsp90.4 mutants, and those subjected to Glyoxalase I inhibitor (S-p-bromobenzylglutathione cyclopentyl diester (BBGD) treatment) reveal that CYS acts as a positive regulator of the GLX system by boosting the activities of Glyoxalase I (GLXI) and Glyoxalase II (GLXII) enzymes involved in methylglyoxal (MG) detoxification, particularly in conjunction with HSP90.1 and HSP90.4. The effects of GLXI inhibitor on the GLX system were experimentally studied for the first time on plants by applying to A. thaliana seedlings (Col-0 and hsp90.4 mutant). Moreover, CYS treatment enhances the expression of genes related to the GLX system and HSPs, leading to improved thermotolerance in A. thaliana. In conclusion, our findings highlight a synergistic interaction between CYS, the GLX system, and HSP90 proteins, suggesting promising genetic and chemical approaches for enhancing plant tolerance to high-temperature stress. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s12298-026-01710-w.

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