Hydrogen sulfide maintains redox homeostasis and suppresses ganoderic acids biosynthesis under heat stress via S-sulfhydrating thioredoxin 1 in Ganoderma lucidum

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Abstract

Abstract Hydrogen sulfide (H 2 S) is considered to be a novel gaseous signalling molecule with multiple physiological functions. Recently, the identification of sulfhydrated proteins has become a new hotspot in the analysis of the underlying mechanism of H 2 S. Our preliminary study has shown that H 2 S negatively regulates the heat-induced accumulation of ganoderic acids (GAs)，a major secondary metabolite in Ganoderma lucidum. However, a comprehensive understanding of its mechanism is lacking. In this study, sulfhydrated proteins in G. lucidum were quantified by quantitative proteomic mass spectrometry (MS), and the role of H 2 S in maintaining redox homeostasis under heat stress (HS) was determined. A redox-regulated protein, thioredoxin 1 (Trx1), was selected as a potential target of H 2 S. Further research revealed that the activity of Trx1 was provoked by sulfhydration at Cys31 and Cys34, contributing to the negative regulation of H 2 S to ROS accumulation and GAs biosynthesis under HS in G. lucidum. Our results provide a novel target for investigating the molecular mechanism of H 2 S physiological function. Moreover, new evidence is provided regarding the interaction mechanism between the H 2 S and ROS signalling pathways.