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Identification of three enzymes of the vanillin and vanillic acid metabolic pathway in the filamentous fungi Aspergillus niger

ABSTRACT: Identification of three enzymes of the vanillin and vanillic acid metabolic pathway in the filamentous fungi Aspergillus niger

PROVIDER: PRJNA647743 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12282446.fastq.gz	Fastqsanger.gz
	SRR12282447.fastq.gz	Fastqsanger.gz
	SRR12282448.fastq.gz	Fastqsanger.gz
	SRR12282449.fastq.gz	Fastqsanger.gz
	SRR12282450.fastq.gz	Fastqsanger.gz

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Identification of three enzymes of the vanillin and vanillic acid metabolic pathway in the filamentous fungi Aspergillus niger

Project description:The aim of this study was to find candidate genes in A. niger involved in the vanillic acid metabolic pathway.

2021-08-11 | GSE154865 | GEO

Secretome analysis of biomass degrading filamentous fungi

Project description:Filamentous fungi are widely used in the production of biomass degrading enzymes, e.g. cellulases and pectinases. In order to study the secretome of biomass degrading fungi, proteomics studies were carried out on the extracellular proteins of fungal strains.

2024-01-03 | PXD048232 |

filamentous fungi

Project description:filamentous fungi Targeted loci cultured

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Project description:The transcriptional activator XlnR (Xlr1/Xyr1) is a major regulator in fungal xylan and cellulose degradation as well as in the utilization of d-xylose via the pentose catabolic pathway. XlnR homologs are commonly found in filamentous ascomycetes and often assumed to have the same function in different fungi. However, a comparison of the saprobe Aspergillus niger and the plant pathogen Magnaporthe oryzae showed different phenotypes for deletion strains of XlnR. In this study wild type and xlnR/xlr1/xyr1 mutants of five fungi were compared: Fusarium graminearum, M. oryzae, Trichoderma reesei, A. niger and Aspergillus nidulans. Growth profiling on relevant substrates and a detailed analysis of the secretome as well as extracellular enzyme activities demonstrated a common role of this regulator in activating genes encoding the main xylanolytic enzymes. However, large differences were found in the set of genes that is controlled by XlnR in the different species, resulting in the production of different extracellular enzyme spectra by these fungi. This comparison emphasizes the functional diversity of a fine-tuned (hemi-)cellulolytic regulatory system in filamentous fungi, which might be related to the adaptation of fungi to their specific biotopes.

2014-08-01 | PXD001190 | Pride

PFK2/FBPase-2 is a potential target for metabolic engineering in the filamentous fungus Myceliophthora thermophila

Project description:The PFK-2/ FBPase-2 are important regulatory enzymes in the glycolytic and are present in all major eukaryotic taxa. However, unlike the well-studied animal and plant PFK-2/ FBPase-2, their functions in filamentous fungi remain little investigated. As a typical filamentous fungus and industrial microorganisms, M. thermophila was choose to investigate the functions of this gene. At the same time, the application of regulating this gene in improving metabolites production was also studied.

2022-09-28 | GSE214142 | GEO

Interspecies and intersubstrate comparison of the biomass-degrading capacity of five filamentous fungi

Project description:The efficiency of microorganisms to degrade lignified plants is of great importance in Earth’s carbon cycle, but also in industrial biorefinery processes, such as for biofuel production. Here, we present a large-scale proteomics approach to investigate and compare the enzymatic response of five filamentous fungi when grown on five very different substrates: bagasse, birch, spruce, cellulose and glucose. The five fungi included the ascomycetes Aspergillus terreus, Hypocrea jecorina, Myceliophthora thermophila, Neurospora crassa and the white-rot basidiomycete Phanerochaete chrysosporium, all expressing a diverse repertoire of enzymes. Many studies have previously been performed with these fungi under various growth conditions, but this study is unique as it presents comparable quantitative protein abundance values across five filamentous fungi and five diverse substrates that allows for direct comparison of fungal response to the different substrates; this approach gives indications to substrate specificity of individual carbohydrate-active enzymes (CAZymes) and identifies several novel co-expressed non-CAZymes. Specifically, we present a quantitative comparison of 34 lytic polysaccharide monooxidenases (LPMOs), which are crucial enzymes in biomass deconstruction.

2020-11-25 | PXD011166 | Pride

Genome-wide transcriptional response of the filamentous fungus Trichoderma reesei to lignocellulose using RNA sequencing and comparison with Aspergillus niger

Project description:The induction of genes in response to exposure of T. reesei to wheat straw was explored using genome-wide RNA-seq and compared to published RNA-seq data and model of how A. niger senses and responds to the lignocellulose. After 24 h of exposure to straw, transcript levels of known and predicted lignocellulose-degrading enzymes increased to around 8% of total cellular mRNA in T. reesei, which was much less when compared to A. niger. The bulk of enzymes used to deconstruct wheat straw is similar in both fungi. Other, non-plant cell wall-degrading enzymes which may aid in lignocellulose degradation were also uncovered in T. reesei and similar to those described in A. niger. Antisense transcripts were also shown to be present in T. reesei and their expession can be regulated by the respective growth condition.

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Genome-wide transcriptional response of the filamentous fungus Trichoderma reesei to lignocellulose using RNA sequencing and comparison with Aspergillus niger

2013-04-01 | E-GEOD-44648 | biostudies-arrayexpress

Application of carbohydrate arrays coupled with mass spectrometry to detect activity of plant-polysaccharide degradative enzymes from the fungus Aspergillus niger

Project description:Renewables-based biotechnology depends on enzymes to degrade plant lignocellulose to simple sugars that are converted to fuels or high-value products. Identification and characterization of such lignocellulose degradative enzymes could be fast-tracked by availability of an enzyme activity measurement method that is fast, label-free, uses minimal resources and allows direct identification of generated products. We developed such a method by applying carbohydrate arrays coupled with MALDI-ToF mass spectrometry to identify reaction products of carbohydrate active enzymes (CAZymes) of the filamentous fungus Aspergillus niger. We describe the production and characterization of plant polysaccharide-derived oligosaccharides and their attachment to hydrophobic self-assembling monolayers on a gold target. We verify effectiveness of this array for detecting exo- and endo-acting glycoside hydrolase activity using commercial enzymes, and demonstrate how this platform is suitable for detection of enzyme activity in relevant biological samples, the culture filtrate of A. niger grown on wheat straw. In conclusion, this versatile method is broadly applicable in screening and characterisation of activity of CAZymes, such as fungal enzymes for plant lignocellulose degradation with relevance to biotechnological applications as biofuel production, the food and animal feed industry.

2018-10-26 | PXD005699 | Pride

Cyclophilin acts as a ribosome biogenesis factor by chaperoning the ribosomal protein in filamentous fungi

Project description:The rapid transport of ribosomal proteins (RPs) into the nucleus and their efficient assembly into rRNA are prerequisites for ribosome biogenesis. Proteins that act as dedicated chaperones for RPs to maintain their stability and facilitate their assembly have not been identified in filamentous fungi. PlCYP5 is a nuclear cyclophilin in the nematophagous fungus Purpureocillium lilacinum, and up-regulated expression in response to abiotic stress and nematode egg-parasitism. Here, we found that PlCYP5 interacted with the unassembled small ribosomal subunit protein, PlRPS15, of the uS19 family. PlRPS15 contained a eukaryote-specific N-terminal extension that mediated the interaction. The phenotypes of the PlCYP5 loss-of-function mutant were similar to those of the PlRPS15 knockdown mutant (e.g., growth and ribosome biogenesis defects). PlCYP5 maintained the solubility of PlRPS15 independent of its catalytic peptide-prolyl isomerase function and supported the integration of PlRPS15 into pre-ribosomes. PlCYP5 homologs in Arabidopsis thaliana, Homo sapiens, Schizosaccharomyces pombe, Sclerotinia sclerotiorum, Botytis cinerea, and Metarhizium anisopliae were identified. Notably, the interaction of their homologs corresponding to the PlCYP5-PlRPS15 pattern existed in three filamentous fungi, while lacked in other species. In summary, our data disclosed a special RP dedicated chaperone system in filamentous fungi, in which cyclophilin was enlisted to perform the chaperone funtion.

2021-07-10 | GSE179712 | GEO

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