Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides
Cysteine persulfide (CysSSH) and cysteine polysulfides (CysSS<sub>n</sub>H, <i>n</i> > 1) are cysteine derivatives that have sulfane sulfur atoms bound to cysteine thiol. Advances in analytical methods that detect and quantify persulfides and polysulfides have shown that C...
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MDPI AG
2020-08-01
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author | Tomohiro Sawa Hozumi Motohashi Hideshi Ihara Takaaki Akaike |
author_facet | Tomohiro Sawa Hozumi Motohashi Hideshi Ihara Takaaki Akaike |
author_sort | Tomohiro Sawa |
collection | DOAJ |
description | Cysteine persulfide (CysSSH) and cysteine polysulfides (CysSS<sub>n</sub>H, <i>n</i> > 1) are cysteine derivatives that have sulfane sulfur atoms bound to cysteine thiol. Advances in analytical methods that detect and quantify persulfides and polysulfides have shown that CysSSH and related species such as glutathione persulfide occur physiologically and are prevalent in prokaryotes, eukaryotes, and mammals in vivo. The chemical properties and abundance of these compounds suggest a central role for reactive persulfides in cell-regulatory processes. CysSSH and related species have been suggested to act as powerful antioxidants and cellular protectants and may serve as redox signaling intermediates. It was recently shown that cysteinyl-tRNA synthetase (CARS) is a new cysteine persulfide synthase. In addition, we discovered that CARS is involved in protein polysulfidation that is coupled with translation. Mitochondrial activity in biogenesis and bioenergetics is supported and upregulated by CysSSH derived from mitochondrial CARS. In this review article, we discuss the mechanisms of the biosynthesis of CysSSH and related persulfide species, with a particular focus on the roles of CARS. We also review the antioxidative and anti-inflammatory actions of persulfides. |
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issn | 2218-273X |
language | English |
last_indexed | 2024-03-10T16:45:42Z |
publishDate | 2020-08-01 |
publisher | MDPI AG |
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series | Biomolecules |
spelling | doaj.art-490a6222cb804905b1d5aa5600c783332023-11-20T11:36:36ZengMDPI AGBiomolecules2218-273X2020-08-01109124510.3390/biom10091245Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and PolysulfidesTomohiro Sawa0Hozumi Motohashi1Hideshi Ihara2Takaaki Akaike3Department of Microbiology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto 860-8556, JapanDepartment of Gene Expression Regulation, Institute of Development, Aging and Cancer, Tohoku University, Miyagi 980-8575, JapanDepartment of Biological Science, Graduate School of Science, Osaka Prefecture University, Osaka 599-8531, JapanDepartment of Environmental Medicine and Molecular Toxicology, Tohoku University Graduate School of Medicine, Miyagi 980-8575, JapanCysteine persulfide (CysSSH) and cysteine polysulfides (CysSS<sub>n</sub>H, <i>n</i> > 1) are cysteine derivatives that have sulfane sulfur atoms bound to cysteine thiol. Advances in analytical methods that detect and quantify persulfides and polysulfides have shown that CysSSH and related species such as glutathione persulfide occur physiologically and are prevalent in prokaryotes, eukaryotes, and mammals in vivo. The chemical properties and abundance of these compounds suggest a central role for reactive persulfides in cell-regulatory processes. CysSSH and related species have been suggested to act as powerful antioxidants and cellular protectants and may serve as redox signaling intermediates. It was recently shown that cysteinyl-tRNA synthetase (CARS) is a new cysteine persulfide synthase. In addition, we discovered that CARS is involved in protein polysulfidation that is coupled with translation. Mitochondrial activity in biogenesis and bioenergetics is supported and upregulated by CysSSH derived from mitochondrial CARS. In this review article, we discuss the mechanisms of the biosynthesis of CysSSH and related persulfide species, with a particular focus on the roles of CARS. We also review the antioxidative and anti-inflammatory actions of persulfides.https://www.mdpi.com/2218-273X/10/9/1245cysteine persulfideantioxidantanti-inflammatory effectsulfur respirationoxidative stresscysteinyl-tRNA synthetase |
spellingShingle | Tomohiro Sawa Hozumi Motohashi Hideshi Ihara Takaaki Akaike Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides Biomolecules cysteine persulfide antioxidant anti-inflammatory effect sulfur respiration oxidative stress cysteinyl-tRNA synthetase |
title | Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides |
title_full | Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides |
title_fullStr | Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides |
title_full_unstemmed | Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides |
title_short | Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides |
title_sort | enzymatic regulation and biological functions of reactive cysteine persulfides and polysulfides |
topic | cysteine persulfide antioxidant anti-inflammatory effect sulfur respiration oxidative stress cysteinyl-tRNA synthetase |
url | https://www.mdpi.com/2218-273X/10/9/1245 |
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