Structural features and functional implications of proteins enabling the robustness of Deinococcus radiodurans

Chen, Zijing; Tang, Ying; Hua, Yuejin; Zhao, Ye

doi:10.1016/j.csbj.2020.09.036

Cited by 8 publications

(5 citation statements)

References 91 publications

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“…Consistently, it was reported that a Deinococcus geothermalis mutant lacking the cystine importer system, which is a source of thiols, was more sensitive to an H 2 O 2 treatment [21]. Some studies based on biochemical, pharmacological, or genetic approaches characterised the Trx system in Deinococcus [22][23][24] and indicated that it likely plays an essential role in responses to oxidative stress [25,26]. In a previous review describing Deinococcus antioxidant systems [3], the main TR families were listed, revealing that this bacterial genus possesses a complete Trx system, including a relatively high number of TRs related to Trxs and Prxs.…”

Section: Introductionmentioning

confidence: 73%

Thiol Reductases in Deinococcus Bacteria and Roles in Stress Tolerance

et al. 2022

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Deinococcus 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 Deinococcus 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 Deinococcus. 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. Deinococcus 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 Deinococcus 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 Deinococcus TR representatives very likely constitutes an asset for the maintenance of redox homeostasis in harsh stress conditions.

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Section: Introductionmentioning

confidence: 73%

Thiol Reductases in Deinococcus Bacteria and Roles in Stress Tolerance

et al. 2022

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“…Comparison of the PprI–DdrO response system with the SOS response system reveals distinctions between them. For one thing, the dimerization of the two repressors depends on the interaction from both NTD and CTD, while the interface of DdrO is much more extensive and CTD dependent ( Lu et al, 2019 ; Chen et al, 2020 ). For another, the dissociation of LexA relies on the autocleavage, which is promoted by the stabilization of autocleavage conformation when RecA is activated after sensing DNA damage and form RecA-ssDNA-ATP filaments ( Butala et al, 2008 , 2011 ).…”

Section: Discussionmentioning

confidence: 99%

“…As for the RDRM sequence recognition and binding, both variation of the conserved base pairs and length shortening impaired the binding of DG-DdrO. In conclusion, the extended dimeric interaction in DdrO is essential for binding to RDRM-containing sequences ( Makarova et al, 2007 ; Lu et al, 2019 ; Chen et al, 2020 ). Besides, apart from this NTD dimerization, Arjan de Groot also revealed a CTD dimerization of DdrO that is quite different to the already known XRE family proteins such as SinR ( de Groot et al, 2019 ).…”

Section: Repression and Derepression Mechanisms Of The Ppri–ddro Systmentioning

confidence: 93%

PprI: The Key Protein in Response to DNA Damage in Deinococcus

Hua

2021

Front. Cell Dev. Biol.

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Deoxyribonucleic acid (DNA) damage response (DDR) pathways are essential for maintaining the integrity of the genome when destabilized by various damaging events, such as ionizing radiation, ultraviolet light, chemical or oxidative stress, and DNA replication errors. The PprI–DdrO system is a newly identified pathway responsible for the DNA damage response in Deinococcus, in which PprI (also called IrrE) acts as a crucial component mediating the extreme resistance of these bacteria. This review describes studies about PprI sequence conservation, regulatory function, structural characteristics, biochemical activity, and hypothetical activation mechanisms as well as potential applications.

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“…Deinococcus radiodurans , a non-spore-forming gram-positive bacterium, is well known for its extreme resistance to environmental stresses, including ionizing radiation, oxidative stress, and DNA damage. It has been shown that the robustness of this bacterium is the result of multiple mechanisms, e.g ., enhanced DNA repair capabilities, novel DNA damage responses, effective antioxidation systems, and cellular protection of damaged DNA and proteins [ 24 - 26 ]. Whole-genome sequence data reveal that D. radioduran s encodes one HU protein, DrHU ( DR_A0065 ), which is highly expressed from a leaderless mRNA [ 27 ].…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation Regulation of a Histone-like HU Protein from Deinococcus radiodurans

Hou

Zhao

Chen

et al. 2022

PPL

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Background: Histone-like proteins are small molecular weight DNA-binding proteins that are widely distributed in prokaryotes. These proteins have multiple functions in cellular structures and processes, including the morphological stability of the nucleoid, DNA compactness, DNA replication, and DNA repair. Deinococcus radiodurans, an extremophilic microorganism, has extraordinary DNA repair capability and encodes an essential histone-like protein, DrHU. Objective: We aim to investigate the phosphorylation regulation role of a histone-like HU protein from Deinococcus radiodurans. Methods: LC-MS/MS analysis was used to determine phosphorylation site of endogenous DrHU. The predicted structure of DrHU-DNA was obtained from homology modeling (Swiss-model) using Staphylococcus aureus HU-DNA structure (PDB ID: 4QJU) as starting model. Two types of mutant proteins T37E and T37A were generated to explore their DNA binding affinity. Complemented-knockout strategy was used to generate the ΔDrHU/pk-T37A and ΔDrHU/pk-T37E strains for growth curves and phenotypical analyses. Results and Discussion: The phosphorylation site Thr37, which is present in most bacterial HU proteins, is located at the putative protein-DNA interaction interface of DrHU. Compared with the wild-type protein, one in which this threonine is replaced by glutamate to mimic a permanent state of phosphorylation (T37E) showed enhanced double-stranded DNA binding but a weakened protective effect against hydroxyl radical cleavage. Complementation of T37E in a DrHU-knockout strain caused growth defects and sensitized the cells to UV radiation and oxidative stress. Conclusions: Phosphorylation modulates the DNA-binding capabilities of the histone-like HU protein from D. radiodurans, which contributes to the environmental adaptation of this organism.

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Structural features and functional implications of proteins enabling the robustness of Deinococcus radiodurans

Cited by 8 publications

References 91 publications

Thiol Reductases in Deinococcus Bacteria and Roles in Stress Tolerance

Thiol Reductases in Deinococcus Bacteria and Roles in Stress Tolerance

PprI: The Key Protein in Response to DNA Damage in Deinococcus

Phosphorylation Regulation of a Histone-like HU Protein from Deinococcus radiodurans

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