Thiol Reductases in <i>Deinococcus</i> Bacteria and Roles in Stress Tolerance

<i>Deinococcus</i> species possess remarkable tolerance to extreme environmental conditions that generate oxidative damage to macromolecules. Among enzymes fulfilling key functions in metabolism regulation and stress responses, thiol reductases (TRs) harbour catalytic cysteines modulatin...

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Main Authors: Arjan de Groot (Author), Laurence Blanchard (Author), Nicolas Rouhier (Author), Pascal Rey (Author)
Format: Book
Published: MDPI AG, 2022-03-01T00:00:00Z.
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042 |a dc 
100 1 0 |a Arjan de Groot  |e author 
700 1 0 |a Laurence Blanchard  |e author 
700 1 0 |a Nicolas Rouhier  |e author 
700 1 0 |a Pascal Rey  |e author 
245 0 0 |a Thiol Reductases in <i>Deinococcus</i> Bacteria and Roles in Stress Tolerance 
260 |b MDPI AG,   |c 2022-03-01T00:00:00Z. 
500 |a 10.3390/antiox11030561 
500 |a 2076-3921 
520 |a <i>Deinococcus</i> species possess remarkable tolerance to extreme environmental conditions that generate oxidative damage to macromolecules. Among enzymes fulfilling key functions in metabolism regulation and stress responses, thiol reductases (TRs) harbour catalytic cysteines modulating the redox status of Cys and Met in partner proteins. We present here a detailed description of <i>Deinococcus</i> TRs regarding gene occurrence, sequence features, and physiological functions that remain poorly characterised in this genus. Two NADPH-dependent thiol-based systems are present in <i>Deinococcus</i>. One involves thioredoxins, disulfide reductases providing electrons to protein partners involved notably in peroxide scavenging or in preserving protein redox status. The other is based on bacillithiol, a low-molecular-weight redox molecule, and bacilliredoxin, which together protect Cys residues against overoxidation. <i>Deinococcus</i> species possess various types of thiol peroxidases whose electron supply depends either on NADPH via thioredoxins or on NADH via lipoylated proteins. Recent data gained on deletion mutants confirmed the importance of TRs in <i>Deinococcus</i> tolerance to oxidative treatments, but additional investigations are needed to delineate the redox network in which they operate, and their precise physiological roles. The large palette of <i>Deinococcus</i> TR representatives very likely constitutes an asset for the maintenance of redox homeostasis in harsh stress conditions. 
546 |a EN 
690 |a <i>Deinococcus</i> 
690 |a thiol 
690 |a reductase 
690 |a peroxidase 
690 |a cysteine 
690 |a oxidative stress 
690 |a Therapeutics. Pharmacology 
690 |a RM1-950 
655 7 |a article  |2 local 
786 0 |n Antioxidants, Vol 11, Iss 3, p 561 (2022) 
787 0 |n https://www.mdpi.com/2076-3921/11/3/561 
787 0 |n https://doaj.org/toc/2076-3921 
856 4 1 |u https://doaj.org/article/8e63242cc33f40a28c3b2c9098f54f9f  |z Connect to this object online.