Specificity of Fur Binding to the Oxidative Stress Response Gene Promoter in the Facultative Anaerobic Archaeon &lt;i&gt;Thermoplasma volcanium&lt;/i&gt;

Minoshima, Hikari; Ikeda, Yu; Fujii, Miki; Satoh, Miho; Ishikawa, Tomoaki; Itoh, Youichi; Kawashima-Ohya, Yoshie; Takano, Koji; Omata, Yoshiaki; Kawashima, Tomokazu

doi:10.1248/bpb.b13-00613

Cited by 4 publications

(3 citation statements)

References 21 publications

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“…Under excessive iron, however, Fur also plays a role in the positive regulation of genes encoding iron-utilizing enzymes (e.g., SodB, SOD) and iron storage proteins ( Latifi et al, 2009 ). Minoshima et al (2014) demonstrated the role of Fur in enhancing resistance to ROSs by Thermoplasma volcanium, a facultative archaeon. Thus Fur encoded by an ORF (TVN0292) [T .…”

Section: Crosstalk Between Oxidative and Other Stressesmentioning

confidence: 98%

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Adaptive Response of Thermophiles to Redox Stress and Their Role in the Process of dye Degradation From Textile Industry Wastewater

2022

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Release of dye-containing textile wastewater into the environment causes severe pollution with serious consequences on aquatic life. Bioremediation of dyes using thermophilic microorganisms has recently attracted attention over conventional treatment techniques. Thermophiles have the natural ability to survive under extreme environmental conditions, including high dye concentration, because they possess stress response adaptation and regulation mechanisms. Therefore, dye detoxification by thermophiles could offer enormous opportunities for bioremediation at elevated temperatures. In addition, the processes of degradation generate reactive oxygen species (ROS) and subject cells to oxidative stress. However, thermophiles exhibit better adaptation to resist the effects of oxidative stress. Some of the major adaptation mechanisms of thermophiles include macromolecule repair system; enzymes such as superoxide dismutase, catalase, and glutathione peroxidase; and non-enzymatic antioxidants like extracellular polymeric substance (EPSs), polyhydroxyalkanoates (PHAs), etc. In addition, different bacteria also possess enzymes that are directly involved in dye degradation such as azoreductase, laccase, and peroxidase. Therefore, through these processes, dyes are first degraded into smaller intermediate products finally releasing products that are non-toxic or of low toxicity. In this review, we discuss the sources of oxidative stress in thermophiles, the adaptive response of thermophiles to redox stress and their roles in dye removal, and the regulation and crosstalk between responses to oxidative stress.

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Section: Crosstalk Between Oxidative and Other Stressesmentioning

confidence: 98%

“…Thus Fur encoded by an ORF (TVN0292) [T . volcanium Fur protein (TvFur)] resists excessive iron accumulation ( Minoshima et al, 2014 ).…”

Section: Crosstalk Between Oxidative and Other Stressesmentioning

confidence: 99%

Adaptive Response of Thermophiles to Redox Stress and Their Role in the Process of dye Degradation From Textile Industry Wastewater

2022

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“…In the process of genomic SELEX experiments using a ferric uptake regulatory protein, TvFur, we found that TvFur binds the promoter region of TVG_RS00310 ( TVN0061 ), which encodes superoxide dismutase, TvSOD [ 18 ]. The TvSOD gene is located at the 5′ end of an operon.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Thermostable 8-Oxoguanine DNA Glycosylase Specific for GO/N Mismatches from the Thermoacidophilic ArchaeonThermoplasma volcanium

Fujii

Hata

Ukita

et al. 2016

Archaea

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The oxidation of guanine (G) to 7,8-dihydro-8-oxoguanine (GO) forms one of the major DNA lesions generated by reactive oxygen species (ROS). The GO can be corrected by GO DNA glycosylases (Ogg), enzymes involved in base excision repair (BER). Unrepaired GO induces mismatched base pairing with adenine (A); as a result, the mismatch causes a point mutation, from G paired with cytosine (C) to thymine (T) paired with adenine (A), during DNA replication. Here, we report the characterization of a putative Ogg from the thermoacidophilic archaeon Thermoplasma volcanium. The 204-amino acid sequence of the putative Ogg (TVG_RS00315) shares significant sequence homology with the DNA glycosylases of Methanocaldococcus jannaschii (MjaOgg) and Sulfolobus solfataricus (SsoOgg). The six histidine-tagged recombinant TVG_RS00315 protein gene was expressed in Escherichia coli and purified. The Ogg protein is thermostable, with optimal activity near a pH of 7.5 and a temperature of 60°C. The enzyme displays DNA glycosylase, and apurinic/apyrimidinic (AP) lyase activities on GO/N (where N is A, T, G, or C) mismatch; yet it cannot eliminate U from U/G or T from T/G, as mismatch glycosylase (MIG) can. These results indicate that TvoOgg-encoding TVG_RS00315 is a member of the Ogg2 family of T. volcanium.

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The mitochondria chronicles of melatonin and ATP: Guardians of phase separation

Loh,

Reiter

2024

Mitochondrial Communications

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Specificity of Fur Binding to the Oxidative Stress Response Gene Promoter in the Facultative Anaerobic Archaeon <i>Thermoplasma volcanium</i>

Cited by 4 publications

References 21 publications

Adaptive Response of Thermophiles to Redox Stress and Their Role in the Process of dye Degradation From Textile Industry Wastewater

Adaptive Response of Thermophiles to Redox Stress and Their Role in the Process of dye Degradation From Textile Industry Wastewater

Characterization of a Thermostable 8-Oxoguanine DNA Glycosylase Specific for GO/N Mismatches from the Thermoacidophilic ArchaeonThermoplasma volcanium

The mitochondria chronicles of melatonin and ATP: Guardians of phase separation

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