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...

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Autores principales:	Melanie Hillion, Marcel Imber, Brandán Pedre, Jörg Bernhardt, Malek Saleh, Vu Van Loi, Sandra Maaß, Dörte Becher, Leonardo Astolfi Rosado, Lorenz Adrian, Christoph Weise, Rüdiger Hell, Markus Wirtz, Joris Messens, Haike Antelmann
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/21e9ed05d56247fb863ba4096fc668dd
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spelling	oai:doaj.org-article:21e9ed05d56247fb863ba4096fc668dd2021-12-02T15:04:59ZThe glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress10.1038/s41598-017-05206-22045-2322https://doaj.org/article/21e9ed05d56247fb863ba4096fc668dd2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05206-2https://doaj.org/toc/2045-2322Abstract 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.Melanie HillionMarcel ImberBrandán PedreJörg BernhardtMalek SalehVu Van LoiSandra MaaßDörte BecherLeonardo Astolfi RosadoLorenz AdrianChristoph WeiseRüdiger HellMarkus WirtzJoris MessensHaike AntelmannNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Melanie Hillion Marcel Imber Brandán Pedre Jörg Bernhardt Malek Saleh Vu Van Loi Sandra Maaß Dörte Becher Leonardo Astolfi Rosado Lorenz Adrian Christoph Weise Rüdiger Hell Markus Wirtz Joris Messens Haike Antelmann The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress
description	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.
format	article
author	Melanie Hillion Marcel Imber Brandán Pedre Jörg Bernhardt Malek Saleh Vu Van Loi Sandra Maaß Dörte Becher Leonardo Astolfi Rosado Lorenz Adrian Christoph Weise Rüdiger Hell Markus Wirtz Joris Messens Haike Antelmann
author_facet	Melanie Hillion Marcel Imber Brandán Pedre Jörg Bernhardt Malek Saleh Vu Van Loi Sandra Maaß Dörte Becher Leonardo Astolfi Rosado Lorenz Adrian Christoph Weise Rüdiger Hell Markus Wirtz Joris Messens Haike Antelmann
author_sort	Melanie Hillion
title	The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress
title_short	The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress
title_full	The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress
title_fullStr	The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress
title_full_unstemmed	The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress
title_sort	glyceraldehyde-3-phosphate dehydrogenase gapdh of corynebacterium diphtheriae is redox-controlled by protein s-mycothiolation under oxidative stress
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/21e9ed05d56247fb863ba4096fc668dd
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The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress

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