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Cerrena unicolor

ABSTRACT: Cerrena unicolor overview

PROVIDER: PRJNA251442 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25153471_1.fastq.gz	Fastqsanger.gz
	SRR25153471_2.fastq.gz	Fastqsanger.gz
	SRR25153472_1.fastq.gz	Fastqsanger.gz
	SRR25153472_2.fastq.gz	Fastqsanger.gz
	SRR25153473_1.fastq.gz	Fastqsanger.gz

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Project description:In this project, the transcriptomic data was obtained from the 6-day and 10-day submerged cultures of Cerrena unicolor sp. 87613 under PDA media, respectively. C.unicolor is reported to be an important medicinal fungus as well as an efficient laccase producer. Interestingly, C.unicolor sp.87613 presented a highest laccase production with ~420 U/mL at fermentation day 6, while the laccase production was reduced by ~27% at fermentation day 10. Therefore, these collected data were used to unveil the potential regulatory mechanism of laccase production. Besides, these transcriptomic data also provide essential data source for a better understanding of C.unicolor in various aspects.

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Project description:A white rot fungus Cerrena unicolor has been identified as an important source of laccase, unfortunately regulation of this enzyme genes expression is poorly understood. Using 1D and 2D PAGE and LC-MS/MS, laccase isoenzymes were investigated in the liquid filtrate of C. unicolor culture. The level of expression of laccase genes was measured using qPCR. The elevated concentrations of copper and manganese in the medium caused greatest change in genes expression and three laccase transcripts were significantly affected after culture temperature was decreased from 28 to 4 °C or increased to 40 °C. The small differences in the PAGE band intensities of individual laccase proteins were also observed, indicating that given compound affect particular laccase's transcript. Analyses of laccase-specific activity, at all tested conditions, showed the increased activities as compared to the control, suggesting that enzyme is regulated at the post-translational stage. We observed that the aspartic protease purified from C. unicolor, significantly stimulate laccase activity. Moreover, electrochemical analysis of protease-treated laccase sample had 5 times higher redox peaks. The obtained results indicate that laccases released by C. unicolor are regulated at transcriptional, translational, and at the post-translational steps of gene expression helping fungus adapt to the environmental changes.

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