Unknown

Dataset Information

0

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


ABSTRACT: 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 H2O2 and NaOCl resulted in irreversible inactivation due to overoxidation of the active site in vitro. Treatment of GapDH with H2O2 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.

SUBMITTER: Hillion M 

PROVIDER: S-EPMC5504048 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Hillion Melanie M   Imber Marcel M   Pedre Brandán B   Bernhardt Jörg J   Saleh Malek M   Loi Vu Van VV   Maaß Sandra S   Becher Dörte D   Astolfi Rosado Leonardo L   Adrian Lorenz L   Weise Christoph C   Hell Rüdiger R   Wirtz Markus M   Messens Joris J   Antelmann Haike H  

Scientific reports 20170710 1


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. T  ...[more]

Similar Datasets

| S-EPMC5377786 | biostudies-literature
| S-EPMC7281563 | biostudies-literature
| S-EPMC3743725 | biostudies-literature
| S-EPMC2922983 | biostudies-literature
| S-EPMC5462994 | biostudies-literature
| S-EPMC6782921 | biostudies-literature
| S-EPMC3421169 | biostudies-literature
| S-EPMC4919446 | biostudies-literature
| S-EPMC3472982 | biostudies-literature
| S-EPMC8327957 | biostudies-literature