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Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes and functions in post-translational thiol-modification by protein  S -mycothiolation as emerging thiol-protection and redox-regulatory mechanism. Here, we have used shotgun-proteomics to identify 26  S -mycothiolated proteins in the pathogen  Corynebacterium diphtheriae  DSM43989 under hypochlorite stress that are involved in energy metabolism, amino acid and nucleotide biosynthesis, antioxidant functions and translation. The glyceraldehyde-3-phosphate dehydrogenase (GapDH) represents the most abundant  S -mycothiolated protein that was modified at its active site Cys153  in vivo . Exposure of purified GapDH to H 2 O 2  and NaOCl resulted in irreversible inactivation due to overoxidation of the active site  in vitro . Treatment of GapDH with H 2 O 2  or NaOCl in the presence of MSH resulted in  S -mycothiolation and reversible GapDH inactivation  in vitro  which was faster compared to the overoxidation pathway. Reactivation of  S -mycothiolated GapDH could be catalyzed by both, the Trx and the Mrx1 pathways  in vitro , but demycothiolation by Mrx1 was faster compared to Trx. In summary, we show here that  S -mycothiolation can function in redox-regulation and protection of the GapDH active site against overoxidation in  C .  diphtheriae  which can be reversed by both, the Mrx1 and Trx pathways.

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The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress