Hydrogen sulfide maintains redox homeostasis and suppresses ganoderic acids biosynthesis under heat stress via persulfidating thioredoxin 1 in Ganoderma lucidum.

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Citation abstract

Hydrogen sulfide (H 2 S) is regarded as a novel gaseous signalling molecule with multiple physiological functions. Recently, the identification of persulfidated proteins has become a new hotspot in the analysis of the underlying mechanism of H 2 S. The preliminary findings of our study indicate that H 2 S exerts a negative regulatory effect on 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, the persulfidated proteins in G. lucidum were identified by means of quantitative proteomic mass spectrometry, and the role of H 2 S in maintaining redox homeostasis under heat stress conditions was determined. A redox-regulated protein, thioredoxin 1 (Trx1), was identified as a potential regulation mechanism of H 2 S in G. lucidum. Further research revealed that the activity of Trx1 was provoked by persulfidation at Cys31 and Cys34, contributing to the negative regulation of H 2 S to ROS accumulation and GAs biosynthesis under heat stress in G. lucidum. This study presents a new understanding of the physiological function and regulation mechanism of H 2 S in G. lucidum, offering a deeper understanding of the interaction mechanism between the H 2 S and ROS signalling pathways within the organism.