Superoxide dismutase biosynthesis by two thermophilic bacteria

Gligić, Ljubinka; Radulović, Željka; Zavišić, Gordana

doi:10.1016/s0141-0229(00)00302-1

Cited by 8 publications

(6 citation statements)

References 14 publications

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“…4a ). The OAT for SOD NG2215 was 70°C, which is close to that of other thermophile-derived SODs (50–70°C) 17 40 but lower than that of the hyperthermophilic SODs (87–95°C) 14 16 . SODA NG2215 , SOD BSn5 , and SODA BSn5 exhibited mesophilic properties with OATs of 30°C, 35°C and 30°C, respectively.…”

Section: Resultssupporting

confidence: 52%

“…Fortunately, the isolation of thermostable SODs from thermotolerant or thermophilic microorganisms offers a rapid and effective means to address this issue. To date, many thermostable SODs have been identified from thermophiles and hyperthermophiles, such as Aquifex pyrophilus 13 , Sulfolobus solfataricus 14 , Aeropyrum pernix 15 , Pyrobaculum aerophilum 16 , Bacillus stearothermophilus 17 , Chloroflexus aurantiacus 18 , Thermomyces lanuginosus 19 , Bacillus licheniformis 20 , Chaetomium thermophilum 21 , and Thermus thermophilus 22 . Recent efforts to improve the thermal resistance of SODs through chemical modification, gene recombination, and simulated SOD compounds have achieved considerable success 23 24 .…”

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confidence: 99%

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A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs

Wang

Zhang

et al. 2014

Sci Rep

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Superoxide dismutases (SODs), especially thermostable SODs, are widely applied in medical treatments, cosmetics, food, agriculture, and other industries given their excellent antioxidant properties. A novel thermostable cambialistic SOD from Geobacillus thermodenitrificans NG80-2 exhibits maximum activity at 70°C and high thermostability over a broad range of temperatures (20–80°C). Unlike other reported SODs, this enzyme contains an extra repeat-containing N-terminal domain (NTD) of 244 residues adjacent to the conserved functional SODA domain. Deletion of the NTD dramatically decreased its optimum active temperature (OAT) to 30°C and also impaired its thermostability. Conversely, appending the NTD to a mesophilic counterpart from Bacillus subtilis led to a moderately thermophilic enzyme (OAT changed from 30 to 55°C) with improved heat resistance. Temperature-dependant circular dichroism analysis revealed the enhanced conformational stability of SODs fused with this NTD. Furthermore, the NTD also contributes to the stress resistance of host proteins without altering their metal ion specificity or oligomerisation form except for a slight effect on their pH profile. We therefore demonstrate that the NTD confers outstanding thermostability to the host protein. To our knowledge, this is the first discovery of a peptide capable of remarkably improving protein thermostability and provides a novel strategy for bioengineering thermostable SODs.

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Section: Resultssupporting

confidence: 52%

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confidence: 99%

A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs

Wang

Zhang

et al. 2014

Sci Rep

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“…When added with NTD, rSOD Ss exhibited optimal activity at 60 °C, similar to SODs (50–70 °C) derived from thermophilic bacteria such as Thermoascus aurantiacus var. levisporus (Song et al 2009 ) and Bacillus stearothermophilus (Gligic et al 2000 ), although lower than those (85–95 °C) reported from the hyperthermophilic archaea such as Aquifex pyrophilus (Yamano et al 1999 ) and Pyrobaculum aerophilum (Whittaker and Whittaker 2000 ). The rSOD Ss retained 74 % of its maximum activity even at 100 °C (compared to 64 % for SOD Ss ).…”

Section: Resultsmentioning

confidence: 90%

Improving the thermostability and stress tolerance of an archaeon hyperthermophilic superoxide dismutase by fusion with a unique N-terminal domain

Zhu

Wang

2016

SpringerPlus

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The superoxide dismutase from the archaeon Sulfolobus solfataricus (SODSs) is a well-studied hyperthermophilic SOD with crystal structure and possible thermostability factors characterized. Previously, we discovered an N-terminal domain (NTD) in a thermophilic SOD from Geobacillus thermodenitrificans NG80-2 which confers heat resistance on homologous mesophilic SODs. The present study therefore aimed to further improve the thermostability and stress tolerance of SODSs via fusion with this NTD. The recombinant protein, rSODSs, exhibited improved thermophilicity, higher working temperature, improved thermostability, broader pH stability, and enhanced tolerance to inhibitors and organic media than SODSs without any alterations in its oligomerization state. These results suggest that the NTD is an excellent candidate for improving stability of both mesophilic and thermophilic SOD from either bacteria or archaea via simple genetic manipulation. Therefore, this study provides a general, feasible and highly useful strategy for generating extremely thermostable SODs for industrial applications. Electronic supplementary materialThe online version of this article (doi:10.1186/s40064-016-1854-9) contains supplementary material, which is available to authorized users.

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“…The soil in Kuwait, in which C. lancifolius naturally grows and thrives, is moderately alkaline. In addition, Kuwait desert temperatures range from 10 to 50°C, and higher temperatures have been shown to help thermophilic bacteria and fungi thrive and produce antioxidant enzymes; an example of this is the SOD isolated from the thermophilic Geobacillus stearothermophilus (Gligic et al 2000 ; Afzal et al 2011 ). The soil in Kuwait is known to contain a diversity of thermophilic and moderately thermophilic bacteria, in the genera Amycolatopsis , Chelativorans , Isoptericola , Nocardia , Aeribacillus , Aneurinibacillus , Brevibacillus , Geobacillus , Kocuria , Marinobacter , and Paenibacillus (Al-Mailem et al 2015 ).…”

Section: Discussionmentioning

confidence: 99%

Synergistic and concentration-dependent toxicity of multiple heavy metals compared with single heavy metals in Conocarpus lancifolius

Redha

Al-Hasan

Afzal

2021

Environ Sci Pollut Res

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While heavy metals (HMs) naturally occur in soil, anthropogenic activities can increase the level of these toxic elements. Conocarpus lancifolius Engl. (Combretaceae) was investigated as a potential phytoremediator of soils contaminated with HM containing crude oil. This study assessed the potential of C. lancifolius (CL), a locally available plant species in Kuwait, for resolving local issues of the HM-contaminated soils. The absorption, accumulation, and distribution of three toxic HMs (Cd, Ni, and Pb) and essential metals (Fe, Mg, and metalloid Se) were examined, and their role in plant toxicity and tolerance was evaluated. Conocarpus lancifolius plants were exposed to two different concentrations of single and mixed HMs for 30 days. The accumulation of HMs was determined in the roots, leaves, stems, and the soil using ICP/MS. Biomass, soil pH, proline and protein content, and bioaccumulation, extraction, and translocation factors were measured. The bioaccumulation, extraction, and transcription factors were all >1, indicating CC is a hyperaccumulator of HM. The HM accumulation in CL was concentration-dependent and depended on whether the plants were exposed to individual or mixed HMs. The C.C leaves, stems, and roots showed a significant accumulation of antioxidant constituents, such as proline, protein, Fe, Mg, and Se. There was an insignificant increase in the soil pH, and a decrease in plant biomass and a significant increase in protein, and osmoprotective-proline as a result of the interaction of mixed heavy metals that are more toxic than single heavy metals. This study indicates that C. lancifolius is a good candidate for phytoremediation of multiple HM-contaminated soils. Further studies to establish the phyto-physiological effect of multiple heavy metals are warranted.

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Superoxide dismutase biosynthesis by two thermophilic bacteria

Cited by 8 publications

References 14 publications

A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs

A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs

Improving the thermostability and stress tolerance of an archaeon hyperthermophilic superoxide dismutase by fusion with a unique N-terminal domain

Synergistic and concentration-dependent toxicity of multiple heavy metals compared with single heavy metals in Conocarpus lancifolius

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