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Multi-omics insights into the response of Aspergillus parasiticus to long-chain alkanes in relation to polyethylene modification

ABSTRACT: Multi-omics insights into the response of Aspergillus parasiticus to long-chain alkanes in relation to polyethylene modification

PROVIDER: PRJNA1190495 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31507544_1.fastq.gz	Fastqsanger.gz
	SRR31507544_2.fastq.gz	Fastqsanger.gz
	SRR31507545_1.fastq.gz	Fastqsanger.gz
	SRR31507545_2.fastq.gz	Fastqsanger.gz
	SRR31507546_1.fastq.gz	Fastqsanger.gz

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Multi-omics insights into the response of Aspergillus parasiticus to long-chain alkanes in relation to polyethylene modification

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Multi-omics insights into the response of Aspergillus parasiticus to long-chain alkanes in relation to polyethylene modification

Project description:In this study, we employed a multi-omics approach to study the ability of Aspergillus parasiticus MM36, an isolate derived from Tenebrio molitor intestines, to metabolize long-chain alkanes (lcAlk) and secrete enzymes able to modify polyethylene (PE). Following genome sequencing, assembly, and annotation the fungus was grown with hexadecane (C16) or a mixture of long-chain alkanesl (C24 to C36) as carbon sources and secretomes were tested for their ability to modify PE to select timepoints for the multi-omics analysis. The selected conditions were lcAlk after days 2 and 3 and C16 after day 3. Culture supernatants with lcAlk after 3 days contained the most effective secretome in PE functionalization and protein diversity. Proteomic analysis of the secretomes identified a range of induced oxidases potentially involved in lcAlk and PE functionalization. Key enzymes include multicopper oxidases, peroxidases, an unspecific peroxygenase and FAD-dependent monooxygenases. Surfactant proteins facilitating enzymatic and cellular interaction with hydrophobic PE and lcAlk, such as one hydrophobin, three hydrophobic surface-binding proteins (HsbA) and one cerato platanin, were present in all secretomes. Transcriptomic analysis comparing lcAlk to C16 cultures highlighted the enrichment of oxidoreductase activities and carboxylic acid metabolism in both lcAlk days, with transmembrane transporters and transferases predominating on day 2 and biosynthetic processes on day 3. In C16 cultures, hydrolytic enzymes, including esterases, were upregulated alongside Baeyer-Villiger monooxygenases, suggesting a shift toward sub-terminal hydroxylation. Integrating transcriptomic and secretomic data, we propose a mechanism for lcAlk assimilation by A. parasiticus MM36, involving extracellular oxyfunctionalization, hydrocarbon uptake via surface-modifying proteins and channeling through membrane transporters for energy consumption and biosynthesic processes.

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Project description:Aflatoxins are toxic and carcinogenic secondary metabolites produced by the fungi Aspergillus flavus and A. parasiticus. In order to better understand the molecular mechanisms that regulate aflatoxin production, the biosynthesis of the toxin in A. flavus and A. parasticus grown in yeast extract sucrose media supplemented with 50 mM tryptophan (Trp) were examined. A. flavus grown in the presence of 50 mM tryptophan was found to have significantly reduced aflatoxin B1 and B2 biosynthesis, while A. parasiticus cultures had significantly increased B1 and G1 biosynthesis. Microarray analysis of RNA extracted from fungi grown under these conditions revealed seventy seven genes that are expressed significantly different between A. flavus and A. parasiticus, including the aflatoxin biosynthetic genes aflD (nor-1), aflE (norA), and aflO (omtB). It is clear that the regulatory mechanisms of aflatoxin biosynthesis in response to Trp in A. flavus and A. parasiticus are different. These candidate genes may serve as regulatory factors of aflatoxin biosynthesis. Keywords: Aflatoxin, Aspergillus, flavus, Amnio Acids, Tryptophan

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