Cytochrome c peroxidase regulates intracellular reactive oxygen species and methylglyoxal via enzyme activities of erythroascorbate peroxidase and glutathione-related enzymes in Candida albicans

Shin, Young-Ho; Lee, Sungkyoung; Ku, MyungHee; Kwak, Min-Kyu; Kang, Sa-Ouk

doi:10.1016/j.biocel.2017.10.004

Cited by 11 publications

(13 citation statements)

References 81 publications

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“…As mentioned above, S. cerevisiae synthesizes an isomeric D-form of eAsA as a five-carbon homolog of AsA. eAsA has a crucial role in antioxidant activity and cyanide-resistant respiration [60][61][62]. In the antioxidant process, eAsA is oxidized to tert-butylhydroperoxide radical, but not H 2 O 2 , which is reduced by NADH-cytochrome b5 reductase (Mcr1p) and Gtop with DHAR activity [63] as well as by DaMDHAR, considering that MDHAR is capable of reducing a wide range of radicals, including AsA, MDHA, quinone, and phenoxyl radicals [62,64,65].…”

Section: Phenotype-based Stress Resistance Of Damdhar-expressing Yeasmentioning

confidence: 99%

Screening and Genetic Network Analysis of Genes Involved in Freezing and Thawing Resistance in DaMDHAR—Expressing Saccharomyces cerevisiae Using Gene Expression Profiling

Kim

Choi

Son

et al. 2021

Genes

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The cryoprotection of cell activity is a key determinant in frozen-dough technology. Although several factors that contribute to freezing tolerance have been reported, the mechanism underlying the manner in which yeast cells respond to freezing and thawing (FT) stress is not well established. Therefore, the present study demonstrated the relationship between DaMDHAR encoding monodehydroascorbate reductase from Antarctic hairgrass Deschampsia antarctica and stress tolerance to repeated FT cycles (FT2) in transgenic yeast Saccharomyces cerevisiae. DaMDHAR-expressing yeast (DM) cells identified by immunoblotting analysis showed high tolerance to FT stress conditions, thereby causing lower damage for yeast cells than wild-type (WT) cells with empty vector alone. To detect FT2 tolerance-associated genes, 3′-quant RNA sequencing was employed using mRNA isolated from DM and WT cells exposed to FT (FT2) conditions. Approximately 332 genes showed ≥2-fold changes in DM cells and were classified into various groups according to their gene expression. The expressions of the changed genes were further confirmed using western blot analysis and biochemical assay. The upregulated expression of 197 genes was associated with pentose phosphate pathway, NADP metabolic process, metal ion homeostasis, sulfate assimilation, β-alanine metabolism, glycerol synthesis, and integral component of mitochondrial and plasma membrane (PM) in DM cells under FT2 stress, whereas the expression of the remaining 135 genes was partially related to protein processing, selenocompound metabolism, cell cycle arrest, oxidative phosphorylation, and α-glucoside transport under the same condition. With regard to transcription factors in DM cells, MSN4 and CIN5 were activated, but MSN2 and MGA1 were not. Regarding antioxidant systems and protein kinases in DM cells under FT stress, CTT1, GTO, GEX1, and YOL024W were upregulated, whereas AIF1, COX2, and TRX3 were not. Gene activation represented by transcription factors and enzymatic antioxidants appears to be associated with FT2-stress tolerance in transgenic yeast cells. RCK1, MET14, and SIP18, but not YPK2, have been known to be involved in the protein kinase-mediated signalling pathway and glycogen synthesis. Moreover, SPI18 and HSP12 encoding hydrophilin in the PM were detected. Therefore, it was concluded that the genetic network via the change of gene expression levels of multiple genes contributing to the stabilization and functionality of the mitochondria and PM, not of a single gene, might be the crucial determinant for FT tolerance in DaMDAHR-expressing transgenic yeast. These findings provide a foundation for elucidating the DaMDHAR-dependent molecular mechanism of the complex functional resistance in the cellular response to FT stress.

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Section: Phenotype-based Stress Resistance Of Damdhar-expressing Yeasmentioning

confidence: 99%

Screening and Genetic Network Analysis of Genes Involved in Freezing and Thawing Resistance in DaMDHAR—Expressing Saccharomyces cerevisiae Using Gene Expression Profiling

Kim

Choi

Son

et al. 2021

Genes

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“…Cytochrome C peroxidase (CCP) is a protein involved in the oxidative stress response by decreasing reactive oxygen species (ROS), such as hydrogen peroxide [55]. It is known that ROS are continuously formed during aerobic metabolism [56].…”

Section: Other Abundant Proteinsmentioning

confidence: 99%

Proteomic analysis on Aspergillus strains that are useful for industrial enzyme production

Takagi¹,

Kojima²,

Ohashi

2020

Bioscience, Biotechnology, and Biochemistry

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A simple intracellular proteomic study was conducted to investigate the biological activities of Aspergillus niger during industrial enzyme production. A strain actively secreting a heterologous enzyme was compared to a reference strain. In total, 1824 spots on 2-D gels were analyzed using MALDI-TOF MS, yielding 343 proteins. The elevated levels of UPR components, BipA, PDI, and calnexin, and proteins related to ERAD and ROS reduction, were observed in the enzyme-producer. The results suggest the occurrence of these responses in the enzyme-producers. Major glycolytic enzymes, Fba1, EnoA, and GpdA, were abundant but at a reduced level relative to the reference, indicating a potential repression of the glycolytic pathway. Interestingly, it was observed that a portion of over-expressed heterologous enzyme accumulated inside the cells and digested during fermentation, suggesting the secretion capacity of the strain was not enough for completing secretion. Newly identified conservedproteins, likely in signal transduction, and other proteins were also investigated.

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“…During the triosephosphate isomerase reaction of glycolysis pathway, MG is generated as an unavoidable by-product under alkaline conditions from glyceraldehyde or dihydroxyacetone [3,4]. Accumulation of MG causes damage to nucleic acids and proteins in eukaryotic cells by irreversibly forming advanced glycation end products during glucose and fructose catalytic metabolism and producing bioactive free radicals [5][6][7].…”

Section: Instructionmentioning

confidence: 99%

Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from Candida Albicans

et al. 2019

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Gre2 is a key enzyme in the methylglyoxal detoxification pathway; it uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde. This enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily whose members catalyze this type of reaction with a broad range of substrates. To elucidate the structural features, we determined the crystal structures of the NADPH-dependent methylglyoxal reductase Gre2 from Candida albicans (CaGre2) for both the apo-form and NADPH-complexed form at resolutions of 2.8 and 3.02 Å, respectively. The CaGre2 structure is composed of two distinct domains: the N-terminal cofactor-binding domain and the C-terminal substrate-binding domain. Extensive comparison of CaGre2 with its homologous structures reveals conformational changes in α12 and β3′ of the NADPH-complex forms. This study may provide insights into the structural and functional variation of SDR family proteins.

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Cytochrome c peroxidase regulates intracellular reactive oxygen species and methylglyoxal via enzyme activities of erythroascorbate peroxidase and glutathione-related enzymes in Candida albicans

Cited by 11 publications

References 81 publications

Screening and Genetic Network Analysis of Genes Involved in Freezing and Thawing Resistance in DaMDHAR—Expressing Saccharomyces cerevisiae Using Gene Expression Profiling

Screening and Genetic Network Analysis of Genes Involved in Freezing and Thawing Resistance in DaMDHAR—Expressing Saccharomyces cerevisiae Using Gene Expression Profiling

Proteomic analysis on Aspergillus strains that are useful for industrial enzyme production

Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from Candida Albicans

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