PRMT5 promotes cellulase production by regulating the expression of cellulase gene eg2 through histone methylation in Ganoderma lucidum

Summary

Scientists discovered that a protein called PRMT5 in Ganoderma lucidum mushroom plays a key role in producing cellulase enzymes that break down plant cellulose. By controlling a specific gene (eg2) through a process called histone methylation, PRMT5 increases cellulase production. This finding could help develop more efficient ways to convert agricultural waste like corn straw into useful sugars for biofuels and other industrial products.

Background

Cellulase enzymes degrade cellulose into reducing sugars with applications in textile, paper, feed, food and energy industries. Ganoderma lucidum is a white rot fungus that secretes large amounts of cellulase during growth. Post-translational modifications have been shown to affect cellulase production in fungi.

Objective

To investigate whether and how protein arginine methyltransferase 5 (PRMT5) is involved in regulating cellulase production in G. lucidum, specifically through histone methylation mechanisms.

Results

Silencing prmt5 reduced cellulase activity by 23%, decreased mycelial growth rate by 71% in wood tubes, and reduced corn straw and corn cob degradation by 60% and 51% respectively. PRMT5 positively regulated eg2 expression through H4R3me2s histone methylation at the promoter and ORF regions. eg2 expression directly affected cellulase activity and agricultural waste degradation ability.

Conclusion

PRMT5 promotes cellulase production in G. lucidum by positively regulating endoglucanase 2 (eg2) expression through histone H4 arginine 3 symmetric dimethylation. This finding provides a theoretical basis for improving cellulase production and developing high-performance enzyme sources for industrial applications.
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