Melanoidin-containing wastewaters induce selective laccase gene expression in the white-rot fungus Trametes sp. I-62

2008 ◽  
Vol 159 (2) ◽  
pp. 103-109 ◽  
Author(s):  
Tania González ◽  
María Carmen Terrón ◽  
Susana Yagüe ◽  
Howard Junca ◽  
José María Carbajo ◽  
...  
2012 ◽  
Vol 78 (16) ◽  
pp. 5845-5854 ◽  
Author(s):  
Yang Yang ◽  
Fangfang Fan ◽  
Rui Zhuo ◽  
Fuying Ma ◽  
Yangmin Gong ◽  
...  

ABSTRACTLaccase is a copper-containing polyphenol oxidase that has great potential in industrial and biotechnological applications. Previous research has suggested that fungal laccase may be involved in the defense against oxidative stress, but there is little direct evidence supporting this hypothesis, and the mechanism by which laccase protects cells from oxidative stress also remains unclear. Here, we report that the expression of the laccase gene from white rot fungus inPichia pastoriscan significantly enhance the resistance of yeast to H2O2-mediated oxidative stress. The expression of laccase in yeast was found to confer a strong ability to scavenge intracellular H2O2and to protect cells from lipid oxidative damage. The mechanism by which laccase gene expression increases resistance to oxidative stress was then investigated further. We found that laccase gene expression inPichia pastoriscould increase the level of glutathione-based antioxidative activity, including the intracellular glutathione levels and the enzymatic activity of glutathione peroxidase, glutathione reductase, and γ-glutamylcysteine synthetase. The transcription of the laccase gene inPichia pastoriswas found to be enhanced by the oxidative stress caused by exogenous H2O2. The stimulation of laccase gene expression in response to exogenous H2O2stress further contributed to the transcriptional induction of the genes involved in the glutathione-dependent antioxidative system, includingPpYAP1,PpGPX1,PpPMP20,PpGLR1, andPpGSH1. Taken together, these results suggest that the expression of the laccase gene inPichia pastoriscan enhance the resistance of yeast to H2O2-mediated oxidative stress by stimulating the glutathione-based antioxidative system to protect the cell from oxidative damage.


2003 ◽  
Vol 69 (12) ◽  
pp. 7083-7090 ◽  
Author(s):  
Tania González ◽  
María C. Terrón ◽  
Ernesto J. Zapico ◽  
Alejandro Téllez ◽  
Susana Yagüe ◽  
...  

ABSTRACT Laccases produced by white rot fungi are involved in the degradation of lignin and a broad diversity of other natural and synthetic molecules, having a great potential for biotechnological applications. They are frequently encoded by gene families, as in the basidiomycete Trametes sp. strain I-62, from which the lcc1, lcc2, and lcc3 laccase genes have been cloned and sequenced. A multiplex reverse transcription-PCR method to simultaneously study the expression of these genes was developed in this study. The assay proved to be quick, simple, highly sensitive, and reproducible and is particularly valuable when numerous samples are to be analyzed and/or if the amount of initial mRNA is limited. It was used to analyze the effect of 3,4-dimethoxybenzyl alcohol (veratryl alcohol) and two of its isomers (2,5-dimethoxybenzyl alcohol and 3,5-dimethoxybenzyl alcohol) on differential laccase gene expression in Trametes sp. strain I-62. These aromatic compounds produced different induction patterns despite their chemical similarity. We found 2,5-dimethoxybenzyl alcohol to be the best inducer of laccase activity while also producing the highest increase in gene expression; 3,5-dimethoxybenzyl alcohol was the next best inducer. Transcript amounts of each gene fluctuated dramatically in the presence of these three inducers, while the total amounts of laccase mRNAs seemed to be modulated by a coordinated regulation of the different genes.


2001 ◽  
Vol 92 (4) ◽  
pp. 372-380 ◽  
Author(s):  
HISASHI HOSHIDA ◽  
MITSUHIDE NAKAO ◽  
HIDENOBU KANAZAWA ◽  
KANAKO KUBO ◽  
TORU HAKUKAWA ◽  
...  

2020 ◽  
Author(s):  
Jianqiao Wang ◽  
Tomohiro Suzuki ◽  
Hideo Dohra ◽  
Toshio Mori ◽  
Hirokazu Kawagishi ◽  
...  

Abstract Background Lignocellulosic biomass is an organic matrix composed of cellulose, hemicellulose, and lignin. In nature, lignin degradation by basidiomycetes is the key step in lignocellulose decay. The white-rot fungus Phanerochaete sordida YK-624 (YK-624) has been extensively studied due to its high lignin degradation ability. In our previous study, it was demonstrated that YK-624 can secrete lignin peroxidase and manganese peroxidase for lignin degradation. However, the underlying mechanism for lignin degradation by YK-624 remains unknown.Results Here, we analyzed YK-624 gene expression following growth under ligninolytic and nonligninolytic conditions and compared the differentially expressed genes in YK-624 to those in the model white-rot fungus P. chrysosporium by next-generation sequencing. More ligninolytic enzymes and lignin-degrading auxiliary enzymes were upregulated in YK-624. This might explain the high degradation efficiency of YK-624. In addition, the genes involved in energy metabolism pathways, such as the TCA cycle, oxidative phosphorylation, lipid metabolism, carbon metabolism and glycolysis, were upregulated under ligninolytic conditions in YK-624.Conclusions In the present study, the first differential gene expression analysis of YK-624 under ligninolytic and nonligninolytic conditions was reported. The results obtained in this study indicated that YK-624 produces more energy- and lignin-degrading enzymes for more efficient lignin biodegradation.


2001 ◽  
Vol 92 (4) ◽  
pp. 372-380 ◽  
Author(s):  
Hisashi Hoshida ◽  
Mitsuhide Nakao ◽  
Hidenobu Kanazawa ◽  
Kanako Kubo ◽  
Toru Hakukawa ◽  
...  

2020 ◽  
Author(s):  
Alex R Gonzalez ◽  
Gino R Corsini ◽  
Sergio Lobos ◽  
Daniela Seelenfreund ◽  
Mario Tello

Abstract Background: Ceriporiopsis subvermispora is a white-rot fungus that displays a high specificity towards lignin mineralization when colonizing dead wood or lignocellulosic compounds. The lignocellulose degrading system from C. subvermispora is formed by genes that encode cellulose hydrolytic enzymes, manganese peroxidases, and laccases that catalyze the efficient depolymerization and mineralization of lignin in the presence of Mn3+ through the formation of lipoperoxides from unsaturated lipid acids. This highly specific lignin-degrading system is unique among white-rot fungi. Methods: In order to determine if this metabolic specialization has modified codon usage of the ligninolytic system, leading to an increased adaptation to the fungal translational machine, we analyzed the adaptation to host codon usage (CAI), tRNA pool (tAI, and AAtAI), codon pair bias (CPB) and the number of effective codons (Nc). These indexes were correlated with gene expression of C. subvermispora, as evaluated by microarray in the presence of two carbon sources, glucose and Aspen wood.Results: General gene expression of C. subvermispora was not correlated with the CAI, tAI, AAtAI, CBP or Nc indexes used to evaluate adaptation to codon bias or the tRNA pool, neither in the presence of glucose or Aspen wood. However, in media containing Aspen wood, the induction of expression of lignin-degrading genes showed a strong correlation with all the former indexes. Lignin-degrading genes, defined as genes whose expression increases at least two-fold in Aspen wood, showed significantly (p<0.001) higher values of CAI, AAtAI, CPB, tAI and lower values of Nc with respect to non-induced genes. Among ligninolytic genes, cellulose-binding proteins and manganese peroxidases presented the highest adaptation values. We also identified an expansion of genes encoding glycine and glutamic acid tRNAs.Conclusions: Our results suggest that the metabolic specialization to use wood as the sole carbon source has introduced a bias in the codon usage of genes involved in lignocellulose degradation. This bias reduces codon diversity and increases codon usage adaptation to the tRNA pool available in C. subvermispora. To our knowledge, this is the first study showing that codon usage is modified to improve the translation efficiency of a group of genes involved in a particular metabolic pathway.


2012 ◽  
Vol 29 ◽  
pp. S94
Author(s):  
O. Pinar ◽  
B. Tetik ◽  
E. Varışlı ◽  
C. Tamerler ◽  
A. Yazgan-Karatas

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