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Aspergillus nidulans FGSC A4

ABSTRACT: Genome-wide analysis of fungal transcriptional regulation by using high-throughput DNA sequencing

PROVIDER: PRJDB4820 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	DRR060253_1.fastq.gz	Fastqsanger.gz
	DRR060253_2.fastq.gz	Fastqsanger.gz
	DRR060254_1.fastq.gz	Fastqsanger.gz
	DRR060254_2.fastq.gz	Fastqsanger.gz
	DRR060255_1.fastq.gz	Fastqsanger.gz

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Aspergillus nidulans FGSC A4

Project description:Genome-wide analysis of fungal transcriptional regulation by using high-throughput DNA sequencing

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Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4.

Project description:Enzymatic conversion of chitin, a β-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varying from the biorefining of chitin-rich waste streams to understanding how medically relevant fungi remodel their chitin-containing cell walls. Although numerous chitinolytic enzymes have been studied in detail, relatively little is known about enzymes capable of deacetylating chitin. We describe the structural and functional characterization of a 237 residue deacetylase (AnCDA) from Aspergillus nidulans FGSC A4. AnCDA acts on chito-oligomers, crystalline chitin, chitosan, and acetylxylan, but not on peptidoglycan. The K m and k cat of AnCDA for the first deacetylation of penta-N-acetyl-chitopentaose are 72 µM and 1.4 s-1, respectively. Combining mass spectrometry and analyses of acetate release, it was shown that AnCDA catalyses mono-deacetylation of (GlcNAc)2 and full deacetylation of (GlcNAc)3-6 in a non-processive manner. Deacetylation of the reducing end sugar was much slower than deacetylation of the other sugars in chito-oligomers. These enzymatic characteristics are discussed in the light of the crystal structure of AnCDA, providing insight into how the chitin deacetylase may interact with its substrates. Interestingly, AnCDA activity on crystalline chitin was enhanced by a lytic polysaccharide monooxygenase that increases substrate accessibility by oxidative cleavage of the chitin chains.

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Aspergillus nidulans FGSC A4

Project description:Transcriptional response of Aspergillus nidulans grown on high and low glucose concentrations

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Project description:Genome-wide analysis of fungal transcriptional regulation by using high-throughput DNA sequencing

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Aspergillus nidulans FGSC A4

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Project description:WGS sequencing, assembly, and annotation

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Aspergillus nidulans FGSC A4

Project description:Aspergillus nidulans FGSC A4 Transcriptome or Gene expression

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Aspergillus nidulans FGSC A4

Project description:Aspergillus nidulans FGSC A4 genome third party annotation and reassembly

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GNPS Aspergillus nidulans FGSC A4 in different media

Project description:Aspergillus nidulans FGSC A4 5 grown in YPD, AF6 and EG:JM media

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Suberin degradation by Aspergillus nidulans

Project description:The study aims essentially at the characterisation of suberin degradation mechanisms by Aspergillus nidulans, at a fundamental level. Suberin is an important protective barrier in plant, thus the study of its biodegradation significantly impacts on phytopatology. In addition, fungal suberin degrading enzymes might provide important insights to develop new waste management, bioremediation and biodeterioration prevention strategies.

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