Relationship between fruiting body development and extracellular laccase production in the edible mushroom Flammulina velutipes.
Ontology highlight
ABSTRACT:
SUBMITTER: Cesur A
PROVIDER: S-EPMC8760411 | biostudies-literature |
REPOSITORIES: biostudies-literature
Similar Datasets
Project description:Twelve Flammulina velutipes strains originating from Poland were identified using internal transcribed spacer (ITS) region sequencing. Based on the sequences obtained, the genomic relationship of the analyzed strains was determined. All F. velutipes strains were also characterized using Biolog FF MicroPlates to obtain data on C-substrate utilization and mitochondrial activity. The ability to decompose various substrates differed among the F. velutipes strains up to five times. The highest catabolic activities were characteristic for only two strains with capabilities to decompose up to 22 carbon sources. The correlation between carbon repression and laccase production by F. velutipes was analyzed based on glucose assimilation by these strains. Moreover, the influence of metal ions (Cu(2+), Cd(2+)), veratric and ferulic acids, and temperature on laccase activities in the analyzed strains was determined. The results obtained proved that all the inducers influenced laccase expression in almost all the analyzed strains. However, the degree of induction depended not only on the strain used but also on the day of the induction.
| S-EPMC4282699 | biostudies-literature
Project description:BackgroundA mycovirus previously identified in brown discolored fruiting bodies of the cultivated mushroom Flammulina velutipes was characterized. We tentatively named the virus the F. velutipes browning virus (FvBV).ResultsPurified FvBV particles contained two dsRNA genomes (dsRNA1 and 2). The complete sequence of dsRNA1 was 1,915 bp long, containing a single open reading frame (ORF) that encoded 580 amino acids of a putative 66-kDa RNA-dependent RNA polymerase (RdRp). dsRNA2 was 1,730 bp long containing a single ORF encoding 541 amino acids of a putative 60-kDa coat protein (CP1). Phylogenetic analysis of the RdRp sequences revealed FvBV to be a Partitivirus, most closely related to Chondrostereum purpureum cryptic virus. An RT-PCR assay was developed for the amplification of a 495-bp cDNA fragment from dsRNA encoding the CP1. When wild F. velutipes isolated from various parts of Japan were examined by RT-PCR assay, three isolates from the central region of Japan contained FvBV. One wild strain infected with FvBV was isolated in Nagano prefecture, where brown discoloration of white cultivated strains has occurred. Fruiting bodies produced by virus-harboring and virus-free F. velutipes were compared.ConclusionsCap color of the fruiting bodies of F. velutipes that contained Partitivirus FvBV was darker than FvBV-free fruiting bodies. The use of RT-PCR enabled association of FvBV and dark brown color of the fruiting body produced by F. velutipes strains.
| S-EPMC3002925 | biostudies-literature
Project description:Phenylalanine ammonia-lyase (PAL) gene is known to be expressed in plants, and is involved in the differentiation, growth and synthesis of secondary metabolites. However, its expression in fungi remains to be explored. To understand its expression in mushroom fungi, the PAL gene of the edible mushroom Flammulina velutipes (Fvpal) was cloned and characterized. The cloned Fvpal consists of 2,175 bp, coding for a polypeptide containing 724 amino acids and having 11 introns. The translated amino acid sequence of Fvpal shares a high identity (66%) with that of ectomycorrhizal fungus Tricholoma matsutake. Distinctively, the Fvpal expression in the mycelium was higher in minimal medium supplemented with L-tyrosine than with other aromatic amino acids. During cultivation of the mushroom on sawdust medium, Fvpal expression in the fruit body correspondingly increased as the mushroom grew. In the fruiting body, Fvpal was expressed more in the stipe than in the pileus. These results suggest that F. velutipes PAL activity differs in the different organs of the mushroom. Overall, this is first report to show that the PAL gene expression is associated with mushroom growth in fungi.
| S-EPMC4630440 | biostudies-literature
Project description:In nature; Flammulina velutipes, also known as winter mushrooms, vary in the color of their fruiting bodies, from black, yellow, pale yellow, or beige to white. The purpose of this study was to compare the genome sequences of different colored strains of F. velutipes and to identify variations in the genes associated with fruiting body color. Comparative genomics of six F. velutipes strains revealed 70 white-strain-specific variations, including single nucleotide polymorphisms (SNPs) and insertions/deletions (indels), in the genome sequences. Among them, 36 variations were located in the open reading frames, and only one variation was identified as a mutation with a disruptive in-frame deletion (ΔGCGCAC) within the annotated gene phenylalanine ammonia-lyase 1 (Fvpal1). This mutation was found to cause a deletion, without a frameshift, of two amino acids at positions 112 and 113 (arginine and threonine, respectively) in the Fvpal1 gene of the white strain. Specific primers to detect this mutation were designed, and amplification refractory mutation system (ARMS) polymerase chain reaction (PCR) was performed to evaluate whether the mutation is color specific for the F. velutipes fruiting body. PCR analysis of a total of 95 F. velutipes strains revealed that this mutation was present only in white strains. In addition, monospores of the heterozygous mutant were isolated, and whether this mutation was related to the color of the fruiting body was evaluated by a mating assay. In the mating analysis of monospores with mutations in Fvpal1, it was found that this mutation plays an important role in determining the color of the fruiting body. Furthermore, the deletion (Δ112RT113) in Fvpal1 is located between motifs that play a key role in the catalytic function of FvPAL1. These results suggest that this mutation can be used as an effective marker for the color-specific breeding of F. velutipes, a representative edible mushroom.
| S-EPMC10053379 | biostudies-literature
Project description:A blight disease of Flammulina velutipes was identified with symptoms of growth cessation of young fruiting bodies, short stipe, and brown spots on the pileus. The pathogenic bacteria were identified as Arthrobacter arilaitensis and Pseudomonas yamanorum by Koch's postulate, gram staining, morphological and 16S ribosomal RNA gene sequence analyses. Either of the pathogenic bacteria or both of them can cause the same symptoms. Transcriptome changes in blighted F. velutipes were investigated between diseased and normal samples. Compared to the control group, 1,099 differentially expressed genes (DEGs) were overlapping in the bacteria-infected groups. The DEGs were significantly enriched in pathways such as xenobiotic metabolism by cytochrome P450 and tyrosine metabolism. Based on weighted correlation network analysis (WGCNA), the module most correlated to the pathogen-treated F. velutipes samples and candidate hub genes in the co-regulatory network were identified. Furthermore, a potential diseased mechanism involved in cell wall non-extension, phenolic substrate oxidation, and stress defense response was proposed based on the up-regulation of differentially expressed genes encoding chitin deacetylase, tyrosinase, cytochrome P450, MFS transporter, and clavaminate synthase-like protein. This study provides insights into the underlying reactions of young fruiting body of F. velutipes suffering from blight disease and facilitates the understanding of the pathogenic procedure of bacteriosis in edible mushrooms.
| S-EPMC6917577 | biostudies-literature
Project description:Arabinogalactan proteins are proteoglycans found on the cell surface and in the cell walls of higher plants. The carbohydrate moieties of most arabinogalactan proteins are composed of β-1,3-galactan main chains and β-1,6-galactan side chains, to which other auxiliary sugars are attached. For the present study, an endo-β-1,3-galactanase, designated FvEn3GAL, was first purified and cloned from winter mushroom Flammulina velutipes. The enzyme specifically hydrolyzed β-1,3-galactan, but did not act on β-1,3-glucan, β-1,3:1,4-glucan, xyloglucan, and agarose. It released various β-1,3-galactooligosaccharides together with Gal from β-1,3-galactohexaose in the early phase of the reaction, demonstrating that it acts on β-1,3-galactan in an endo-fashion. Phylogenetic analysis revealed that FvEn3GAL is member of a novel subgroup distinct from known glycoside hydrolases such as endo-β-1,3-glucanase and endo-β-1,3:1,4-glucanase in glycoside hydrolase family 16. Point mutations replacing the putative catalytic Glu residues conserved for enzymes in this family with Asp abolished activity. These results indicate that FvEn3GAL is a highly specific glycoside hydrolase 16 endo-β-1,3-galactanase.
| S-EPMC3149374 | biostudies-literature
Project description:Flammulina velutipes, one of the most popular mushroom species in the world, has been recognized as a useful model system to study the biochemical and physiological aspects of the formation and elongation of fruit body. However, few reports have been published on the regulation of fruiting body formation in F. velutipes at the molecular level. In this study, a jacalin-related lectin gene from F. velutipes was characterized. The phylogenetic tree revealed that Fv-JRL1 clustered with other basidiomycete jacalin-like lectins. Moreover, the transcriptional pattern of the Fv-JRL1 gene in different developmental stages of F. velutipes implied that Fv-JRL1 could be important for formation of fruit body. Additionally, RNA interference (RNAi) and overexpression analyses provided powerful evidence that the lectin gene Fv-JRL1 from F. velutipes plays important roles in fruiting body formation.
| S-EPMC5187758 | biostudies-literature
Project description:Fungi can produce many compounds, such as proteins, enzymes, amino acids, and polysaccharides, which are internalised and enriched for metals, and are widely used as reducing and stabilising agents for the biosynthesis of gold nanoparticles (Au NPs). Almost all fungal sources used in the synthesis of the Au NPs are in the form of cell filtrates or mycelial suspensions. However, the culture of cell-free fungal filtrate and mycelium is not comparable to the propagation of fungal substrates in input and operation. Here, we evaluated in vivo biosynthesis of Au NPs in enoki mushrooms (Flammulina velutipes). HAuCl4 was reduced in the fruiting body of the enoki mushrooms via induction by Pb2+ , resulting in the generation of Au NPs. We then employed UV-Vis absorption spectroscopy, Transmission Electron Microscope, and Energy Dispersive Spectrometer to characterise various shapes of the Au NPs. The elemental analysis indicated that the Au NPs were mainly concentrated in organelles of the stalk and cap cells. We also demonstrated that 0.3-0.5 mM HAuCl4 was the optimal stress treatment concentration based on the changes in physiological indicators of the enoki mushrooms. This work reveals that fungi can be utilised well as nanomaterial bioreactors.
| S-EPMC10116022 | biostudies-literature
Project description:Flammutoxin has been previously isolated as a cardiotoxic and cytolytic polypeptide of 22 or 32 kDa from the fruiting bodies of the edible mushroom Flammulina velutipes. In the present study, we purified flammutoxin as a single haemolytic protein of 31 kDa and studied the mode of its cytolytic action. (1) Flammutoxin caused efflux of potassium ions from human erythrocytes and swelling of the cells before haemolysis. (2) Flammutoxin did not lyse human erythrocytes in the presence of non-electrolytes with hydrodynamic diameters of >5.0 nm, although it caused leakage of potassium ions and swelling of the cells under the same conditions. (3) Experiments including solubilization of cell-bound toxin with 2% (w/v) SDS at 20 degrees C and subsequent Western immunoblots showed that flammutoxin formed a band corresponding to 180 kDa under the conditions where it lysed erythrocytes. (4) Electron microscopy of flammutoxin-treated human erythrocytes revealed the presence of a ring-shaped structure with outer and inner diameters of 10 and 5 nm, respectively, on the cells. (5) A ring-shaped toxin oligomer of the same dimensions was solubilized from the toxin-treated human erythrocytes with 2% (w/v) SDS at 20 degrees C and isolated by a sucrose-gradient ultracentrifugation. These data indicated that flammutoxin assembles into a ring-shaped oligomer possessing a hydrophilic pore of 4-5 nm on target cells.
| S-EPMC1219565 | biostudies-other
Project description:We isolated a bacterial identified as the genus of Mycetocola from the infected Flammulina velutipes samples collected from mushroom house in Hebei, North China. The stipe of F. velutipes appeared water-soaked, soften and browning after infected, finally, the whole plant rotten. The incidence of the disease can reach more than 80% in the serious areas, resulting in an obvious decline in the yield and quality of the F. velutipes. Furthermore, the pathogenic bacteria may occurrence in large areas by accumulated in the annual cultivation process. Therefore, the most effective measures to control this bacterial disease is screening resistant strains of F. velutipes with high yield and good agronomic traits. We obtained a white F. velutipes strain JK502 which has strong resistance to this bacterium by using the double-layer plate method combined with the sporozoite hybridization. JK501, which can early fruited, was screened using the same parent SH9 by multi spore hybridization. In order to investigate the differences of gene expression between the parent strain and the selected strains, we completed the transcriptome sequencing by Illumina HiSeq X system.
2024-02-21 | GSE111625 | GEO