scholarly journals Transcriptional and Enzymatic Profiling of Pleurotus ostreatus Laccase Genes in Submerged and Solid-State Fermentation Cultures

2012 ◽  
Vol 78 (11) ◽  
pp. 4037-4045 ◽  
Author(s):  
Raúl Castanera ◽  
Gúmer Pérez ◽  
Alejandra Omarini ◽  
Manuel Alfaro ◽  
Antonio G. Pisabarro ◽  
...  
Keyword(s):  
Gene Family ◽  
Wheat Straw ◽  
Pleurotus Ostreatus ◽  
Submerged Fermentation ◽  
Expression Profiles ◽  
Water Soluble ◽  
White Rot ◽  
Accurate Estimation ◽  
Laccase Gene ◽  
Laccase Genes

ABSTRACTThe genome of the white rot basidiomycetePleurotus ostreatusincludes 12 phenol oxidase (laccase) genes. In this study, we examined their expression profiles in different fungal strains under different culture conditions (submerged and solid cultures) and in the presence of a wheat straw extract, which was used as an inducer of the laccase gene family. We used a reverse transcription-quantitative PCR (RT-qPCR)-based approach and focused on determining the reaction parameters (in particular, the reference gene set for the normalization and reaction efficiency determinations) used to achieve an accurate estimation of the relative gene expression values. The results suggested that (i) laccase gene transcription is upregulated in the induced submerged fermentation (iSmF) cultures but downregulated in the solid fermentation (SSF) cultures, (ii) theLacc2andLacc10genes are the main sources of laccase activity in the iSmF cultures upon induction with water-soluble wheat straw extracts, and (iii) an additional, as-yet-uncharacterized activity (Unk1) is specifically induced in SSF cultures that complements the activity of Lacc2 and Lacc10. Moreover, both the enzymatic laccase activities and theLaccgene family transcription profiles greatly differ between closely related strains. These differences can be targeted for biotechnological breeding programs for enzyme production in submerged fermentation reactors.

scholarly journals Expression Profile of Laccase Gene Family in White-Rot Basidiomycete Lentinula edodes under Different Environmental Stresses

Genes ◽  
2019 ◽  
Vol 10 (12) ◽  
pp. 1045
Author(s):  
Lianlian Yan ◽  
Ruiping Xu ◽  
Yinbing Bian ◽  
Hongxian Li ◽  
Yan Zhou
Keyword(s):  
Gene Family ◽  
Fruiting Body ◽  
Lentinula Edodes ◽  
Expression Profiles ◽  
Draft Genome ◽  
White Rot ◽  
Laccase Gene ◽  
Fruiting Body Formation ◽  
Body Formation ◽  
Laccase Genes

Laccases belong to ligninolytic enzymes and play important roles in various biological processes of filamentous fungi, including fruiting-body formation and lignin degradation. The process of fruiting-body development in Lentinula edodes is complex and is greatly affected by environmental conditions. In this paper, 14 multicopper oxidase-encoding (laccase) genes were analyzed in the draft genome sequence of L. edodes strain W1-26, followed by a search of multiple stress-related Cis-elements in the promoter region of these laccase genes, and then a transcription profile analysis of 14 laccase genes (Lelcc) under the conditions of different carbon sources, temperatures, and photoperiods. All laccase genes were significantly regulated by varying carbon source materials. The expression of only two laccase genes (Lelcc5 and Lelcc6) was induced by sodium-lignosulphonate and the expression of most laccase genes was specifically upregulated in glucose medium. Under different temperature conditions, the expression levels of most laccase genes decreased at 39 °C and transcription was significantly increased for Lelcc1, Lelcc4, Lelcc5, Lelcc9, Lelcc12, Lelcc13, and Lelcc14 after induction for 24 h at 10 °C, indicating their involvement in primordium differentiation. Tyrosinase, which is involved in melanin synthesis, was clustered with the same group as Lelcc4 and Lelcc7 in all the different photoperiod treatments. Meanwhile, five laccase genes (Lelcc8, Lelcc9, Lelcc12, Lelcc13, and Lelcc14) showed similar expression profiles to that of two blue light receptor genes (LephrA and LephrB) in the 12 h light/12 h dark treatment, suggesting the involvement of laccase genes in the adaptation process of L. edodes to the changing environment and fruiting-body formation. This study contributes to our understanding of the function of the different Lelcc genes and facilitates the screening of key genes from the laccase gene family for further functional research.

scholarly journals The Soybean Laccase Gene Family: Evolution and Possible Roles in Plant Defense and Stem Strength Selection

Genes ◽  
2019 ◽  
Vol 10 (9) ◽  
pp. 701 ◽  
Author(s):  
Wang ◽  
Li ◽  
Zheng ◽  
Zhu ◽  
Ma ◽  
...  
Keyword(s):  
Gene Family ◽  
Expression Patterns ◽  
Wild Soybean ◽  
Constitutive Expression ◽  
Gene Family Evolution ◽  
Laccase Gene ◽  
Functional Studies ◽  
Stem Strength ◽  
A Genome ◽  
Laccase Genes

Laccase is a widely used industrial oxidase for food processing, dye synthesis, paper making, and pollution remediation. At present, laccases used by industries come mainly from fungi. Plants contain numerous genes encoding laccase enzymes that show properties which are distinct from that of the fungal laccases. These plant-specific laccases may have better potential for industrial purposes. The aim of this work was to conduct a genome-wide search for the soybean laccase genes and analyze their characteristics and specific functions. A total of 93 putative laccase genes (GmLac) were identified from the soybean genome. All 93 GmLac enzymes contain three typical Cu-oxidase domains, and they were classified into five groups based on phylogenetic analysis. Although adjacent members on the tree showed highly similar exon/intron organization and motif composition, there were differences among the members within a class for both conserved and differentiated functions. Based on the expression patterns, some members of laccase were expressed in specific tissues/organs, while some exhibited a constitutive expression pattern. Analysis of the transcriptome revealed that some laccase genes might be involved in providing resistance to oomycetes. Analysis of the selective pressures acting on the laccase gene family in the process of soybean domestication revealed that 10 genes could have been under artificial selection during the domestication process. Four of these genes may have contributed to the transition of the soft and thin stem of wild soybean species into strong, thick, and erect stems of the cultivated soybean species. Our study provides a foundation for future functional studies of the soybean laccase gene family.

Cloning and characterization of a laccase gene from the white-rot basidiomycete Pleurotus ostreatus

Mycoscience ◽  
2003 ◽  
Vol 44 (1) ◽  
pp. 11-17 ◽  
Author(s):  
Kenji Okamoto ◽  
Ichirou Shigematsu ◽  
Hideshi Yanase ◽  
Yasuhiro Ito ◽  
Sonoe Ochiai Yanagi
Keyword(s):  
Pleurotus Ostreatus ◽  
White Rot ◽  
Laccase Gene

scholarly journals Use of Multiplex Reverse Transcription-PCR To Study the Expression of a Laccase Gene Family in a Basidiomycetous Fungus

2003 ◽  
Vol 69 (12) ◽  
pp. 7083-7090 ◽  
Author(s):  
Tania González ◽  
María C. Terrón ◽  
Ernesto J. Zapico ◽  
Alejandro Téllez ◽  
Susana Yagüe ◽  
...  
Keyword(s):  
Gene Expression ◽  
Reverse Transcription ◽  
White Rot Fungi ◽  
Gene Families ◽  
Veratryl Alcohol ◽  
White Rot ◽  
Laccase Gene ◽  
Reverse Transcription Pcr ◽  
Basidiomycetous Fungus ◽  
Laccase Genes

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.

Metal-responsive elements in Pleurotus ostreatus laccase gene promoters

Microbiology ◽  
2003 ◽  
Vol 149 (8) ◽  
pp. 2155-2162 ◽  
Author(s):  
Vincenza Faraco ◽  
Paola Giardina ◽  
Giovanni Sannia
Keyword(s):  
Pleurotus Ostreatus ◽  
Copper Ions ◽  
Protein S ◽  
Start Codon ◽  
Gene Promoters ◽  
Laccase Gene ◽  
Promoter Regions ◽  
Molecular Masses ◽  
Laccase Genes

Fungal laccase gene transcription is strongly induced by copper ions; notably, some laccase promoters contain multiple putative metal-responsive elements (MREs). Previously, it has been demonstrated that the Pleurotus ostreatus laccase genes poxc and poxa1b are transcriptionally induced by copper, and several putative MREs were found in the promoter regions of these genes, which extend for about 400 nt upstream of the start codon (ATG). Identification of MRE sequences, which are protected by protein binding in the poxc and poxa1b promoter regions, has been achieved by footprinting analyses. Electromobility shift assays led to the evaluation of the ability of the identified MREs to bind protein(s), and the role of specific nucleotides of these elements in complex formation has also been analysed. The formation of complexes between analysed MREs and fungal proteins requires the absence of metal ions. Proteins extracted from fungus grown in copper-depleted medium are able to form complexes with MREs, whilst proteins extracted from fungus grown in copper-containing medium are able to form complexes only in the presence of a metal chelator. Moreover, copper-depleted proteins are unable to form complexes when copper or zinc ions are added. UV-cross-linking analyses led to the determination of the molecular masses of the MRE-binding proteins. In the poxa1b promoter, a GC-rich region, homologous to the core binding site for transcription factor Sp1, decreases the binding affinity of the adjacent MRE, affecting its interactions with fungal protein factors.

Induction of laccase activity in the white rot fungus Pleurotus ostreatus using water polluted with wheat straw extracts

2013 ◽  
Vol 133 ◽  
pp. 142-149 ◽  
Author(s):  
Alejandra Parenti ◽  
Elaia Muguerza ◽  
Amaia Redin Iroz ◽  
Alejandra Omarini ◽  
Enma Conde ◽  
...  
Keyword(s):  
Wheat Straw ◽  
Pleurotus Ostreatus ◽  
Laccase Activity ◽  
White Rot ◽  
White Rot Fungus

scholarly journals Effect of textile dyes on activity and differential regulation of laccase genes from Pleurotus ostreatus grown in submerged fermentation

AMB Express ◽  
2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Verónica Garrido-Bazán ◽  
Maura Téllez-Téllez ◽  
Alfredo Herrera-Estrella ◽  
Gerardo Díaz-Godínez ◽  
Soley Nava-Galicia ◽  
...  
Keyword(s):  
Pleurotus Ostreatus ◽  
Submerged Fermentation ◽  
Differential Regulation ◽  
Textile Dyes ◽  
Laccase Genes

scholarly journals Alternative Splicing of Heat Shock Transcription Factor 2 Regulates Expression of the Laccase Gene Family in Response to Copper in Trametes trogii

2021 ◽  
Vol 87 (8) ◽  
Author(s):  
Yu Zhang ◽  
Yuanyuan Wu ◽  
Xulei Yang ◽  
En Yang ◽  
Huini Xu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Alternative Splicing ◽  
Heat Shock ◽  
Gene Family ◽  
White Rot Fungi ◽  
Primary Source ◽  
White Rot ◽  
Laccase Gene ◽  
Splicing Variants ◽  
Trametes Trogii

ABSTRACT White-rot fungi, especially Trametes strains, are the primary source of industrial laccases in bioenergy and bioremediation. Trametes strains express members of the laccase gene family with different physicochemical properties and expression patterns. However, the literature on the expression pattern of the laccase gene family in Trametes trogii S0301 and the response mechanism to Cu2+, a key laccase inducer, in white-rot fungal strains is scarce. In the present study, we found that Cu2+ could induce the mRNAs and proteins of the two alternative splicing variants of heat shock transcription factor 2 (TtHSF2). Furthermore, the overexpression of alternative splicing variants TtHSF2α and TtHSF2β-I in the homokaryotic T. trogii S0301 strain showed opposite effects on the extracellular total laccase activity, with maximum laccase activities of approximately 0.6 and 3.0 U ml−1, respectively, on day 8, which are 0.4 and 2.3 times that of the wild-type strain. Similarly, TtHSF2α and TtHSF2β-I play opposite roles in the oxidation tolerance to H2O2. In addition, the direct binding of TtHSF2α to the promoter regions of the representative laccase isoenzymes (TtLac1 and TtLac13) and protein-protein interactions between TtHSF2α and TtHSF2β-I were detected. Our results demonstrate the crucial roles of TtHSF2 and its alternative splicing variants in response to Cu2+. We believe that these findings will deepen our understanding of alternative splicing of heat shock transcription factors (HSFs) and their regulatory mechanism of the laccase gene family in white-rot fungi. IMPORTANCE The members of laccase gene family in Trametes strains are the primary source of industrial laccase and have gained widespread attention. Increasing the yield and enzymatic properties of laccase through various methods has always been a topic worthy of attention, and there is no report on the regulation of laccase expression through HSF transcription factor engineering. Here, we found that two alternative splicing variants of TtHSF2 functioned oppositely in regulating the expression of laccase genes, and copper can induce the expression of almost all members of the laccase gene family. Most importantly, our study suggested that TtHSF2 and its alternative splicing variants are vital for copper-induced production of laccases in T. trogii S0301.

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