Tolerance to Oxidative Stress in Budding Yeast by Heterologous Expression of Catalases A and T from Debaryomyces hansenii

González, Jesús Salvador; Castillo, R Díaz; García-Campos, Miguel Angel; Noriega-Samaniego, Diego; Escobar‐Sánchez, Viviana; Romero-Aguilar, Lucero; Alba-Lois, Luisa; Segal-Kischinevzky, Claudia

doi:10.1007/s00284-020-02237-3

Cited by 9 publications

(4 citation statements)

References 72 publications

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“…Catalases are predominantly localized within peroxisomes and typically feature a peroxisomal targeting signal (PTS) that directs their specific peroxisome localization. González et al reported that Sc Cta1 and Dh Cta1, catalases from S. cerevisiae and D. hansenii ( 19 ), respectively, have their PTS targeting signals located at the extreme C-terminus of their protein sequences. However, Petrova et al and Rymer et al have noted that other peroxisomal proteins lack the typical PTS1 (SSNSKF) or PTS2 (SKF) signals ( 32 , 33 ).…”

Section: Resultsmentioning

confidence: 99%

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Unveiling the super tolerance of Candida nivariensis to oxidative stress: insights into the involvement of a catalase

Qi,

Qin,

Liao

et al. 2024

Microbiol Spectr

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Yeast cells involved in fermentation processes face various stressors that disrupt redox homeostasis and cause cellular damage, making the study of oxidative stress mechanisms crucial. In this investigation, we isolated a resilient yeast strain, Candida nivariensis GXAS-CN, capable of thriving in the presence of high concentrations of H 2 O 2 . Transcriptomic analysis revealed the up-regulation of multiple antioxidant genes in response to oxidative stress. Deletion of the catalase gene Cncat significantly impacted H 2 O 2 -induced oxidative stress. Enzymatic analysis of recombinant Cn Cat highlighted its highly efficient catalase activity and its essential role in mitigating H 2 O 2 . Furthermore, over-expression of Cn Cat in Saccharomyces cerevisiae improved oxidative resistance by reducing intracellular ROS accumulation. The presence of multiple stress-responsive transcription factor binding sites at the promoters of antioxidative genes indicates their regulation by different transcription factors. These findings demonstrate the potential of utilizing the remarkably tolerant C. nivariensis GXAS-CN or enhancing the resistance of S. cerevisiae to improve the efficiency and cost-effectiveness of industrial fermentation processes. IMPORTANCE Enduring oxidative stress is a crucial trait for fermentation strains. The importance of this research is its capacity to advance industrial fermentation processes. Through an in-depth examination of the mechanisms behind the remarkable H 2 O 2 resistance in Candida nivariensis GXAS-CN and the successful genetic manipulation of this strain, we open the door to harnessing the potential of the catalase Cn Cat for enhancing the oxidative stress resistance and performance of yeast strains. This pioneering achievement creates avenues for fine-tuning yeast strains for precise industrial applications, ultimately leading to more efficient and cost-effective biotechnological processes.

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Section: Resultsmentioning

confidence: 99%

“…By heterologously expressing these genes, it is possible to enhance the tolerance or resistance of S. cerevisiae to oxidative stress. This genetic modification could potentially aid in the adaptation of S. cerevisiae to environmental stresses during the fermentation process ( 19 ).…”

Section: Introductionmentioning

confidence: 99%

Unveiling the super tolerance of Candida nivariensis to oxidative stress: insights into the involvement of a catalase

Qi,

Qin,

Liao

et al. 2024

Microbiol Spectr

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“…The gastric pathogen Helicobacter pylori catalases protect the bacterium against oxidative stress (Benoit and Maier, 2016 ). Heterologously expressed Debaryomyces hansenii DhCTA1 and DhCTT1 genes conferred enhanced tolerance of S. cerevisiae to oxidative stress (González et al, 2020 ). In the present study, PsCAT1 was overexpressed in S. cerevisiae treated with exogenous ROS.…”

Section: Discussionmentioning

confidence: 99%

A secreted catalase contributes to Puccinia striiformis resistance to host-derived oxidative stress

et al. 2021

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Plants can produce reactive oxygen species (ROS) to counteract pathogen invasion, and pathogens have also evolved corresponding ROS scavenging strategies to promote infection and pathogenicity. Catalases (CATs) have been found to play pivotal roles in detoxifying H2O2 formed by superoxide anion catalyzed by superoxide dismutases (SODs). However, few studies have addressed H2O2 removing during rust fungi infection of wheat. In this study, we cloned a CAT gene PsCAT1 from Puccinia striiformis f. sp. tritici (Pst), which encodes a monofunctional heme-containing catalase. PsCAT1 exhibited a high degree of tolerance to pH and temperature, and forms high homopolymers.Heterologous complementation assays in Saccharomyces cerevisiae reveal that the signal peptide of PsCAT1 is functional. Overexpression of PsCAT1 enhanced S. cerevisiae resistance to H2O2. Transient expression of PsCAT1 in Nicotiana benthamiana suppressed Bax-induced cell death. Knockdown of PsCAT1 using a host-induced gene silencing (HIGS) system led to the reduced virulence of Pst, which was correlated to H2O2 accumulation in HIGS plants. These results indicate that PsCAT1 acts as an important pathogenicity factor that facilitates Pst infection by scavenging host-derived H2O2.

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“…Typically, the reactive oxygen species include hydroxyl radical, superoxide, peroxynitrite, hypochlorous acid, nitric oxide, and singlet oxygen [37]. To eliminate reactive oxygen species and survive adverse conditions, microorganisms produce and release reductase (e.g., dehydrogenase, superoxide dismutase, and catalase) to alleviate oxidative stress [38]. The TiO 2 NP addition amounts (R 2 = 83.95%, F = 272.47; p < 0.001) rather than exposure times (R 2 = 2.84%, F = 4.60; p < 0.05) exhibited significant effects on the enzyme activity (Figure 1).…”

Section: Responses Of the Bacterial Community To Tio 2 Np Additionmentioning

confidence: 99%

Sediment Bacteria and Phosphorus Fraction Response, Notably to Titanium Dioxide Nanoparticle Exposure

Piao

2022

Microorganisms

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Titanium dioxide nanoparticle (TiO2 NP) toxicity to the growth of organisms has been gradually clarified; however, its effects on microorganism-mediated phosphorus turnover are poorly understood. To evaluate the influences of TiO2 NPs on phosphorus fractionation and the bacterial community, aquatic microorganisms were exposed to different concentrations of TiO2 NPs with different exposure times (i.e., 0, 10, and 30 days). We observed the adhesion of TiO2 NPs to the cell surfaces of planktonic microbes by using SEM, EDS, and XRD techniques. The addition of TiO2 NPs resulted in a decrease in the total phosphorus of water and an increase in the total phosphorus of sediments. Additionally, elevated TiO2 NPs enhanced the sediment activities of reductases (i.e., dehydrogenase [0.19–2.25 μg/d/g] and catalase [1.06–2.92 μmol/d/g]), and significantly decreased the absolute abundances of phosphorus-cycling-related genes (i.e., gcd [1.78 × 104–9.55 × 105 copies/g], phoD [5.50 × 103–5.49 × 107 copies/g], pstS [4.17 × 102–1.58 × 106 copies/g]), and sediment bacterial diversity. TiO2 NPs could noticeably affect the bacterial community, showing dramatic divergences in relative abundances (e.g., Actinobacteria, Acidobacteria, and Firmicutes), coexistence patterns, and functional redundancies (e.g., translation and transcription). Our results emphasized that the TiO2 NP amount—rather than the exposure time—showed significant effects on phosphorus fractions, enzyme activity, phosphorus-cycling-related gene abundance, and bacterial diversity, whereas the exposure time exhibited a greater influence on the composition and function of the sediment bacterial community than the TiO2 NP amount. Our findings clarify the responses of phosphorus fractions and the bacterial community to TiO2 NP exposure in the water–sediment ecosystem and highlight potential environmental risks of the migration of untreated TiO2 NPs to aquatic ecosystems.

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Tolerance to Oxidative Stress in Budding Yeast by Heterologous Expression of Catalases A and T from Debaryomyces hansenii

Cited by 9 publications

References 72 publications

Unveiling the super tolerance of Candida nivariensis to oxidative stress: insights into the involvement of a catalase

Unveiling the super tolerance of Candida nivariensis to oxidative stress: insights into the involvement of a catalase

A secreted catalase contributes to Puccinia striiformis resistance to host-derived oxidative stress

Sediment Bacteria and Phosphorus Fraction Response, Notably to Titanium Dioxide Nanoparticle Exposure

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