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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Main Authors: Tomohiro Sawa, Hozumi Motohashi, Hideshi Ihara, Takaaki Akaike
Format: Article
Language:English
Published: MDPI AG 2020-08-01
Series:Biomolecules
Subjects:
Online Access:https://www.mdpi.com/2218-273X/10/9/1245
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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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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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