GlSlt2 positively regulates GlMyb-mediated cellulose utilization in Ganoderma lucidum

Summary

Scientists discovered how a medicinal mushroom called Ganoderma lucidum breaks down cellulose from plant waste. The study found that a protein called GlSlt2 activates another protein called GlMyb, which then turns on genes that produce cellulase enzymes. These enzymes break down cellulose into sugar that the fungus can use for growth. This discovery could help improve the conversion of agricultural waste into biofuels and other useful products.

Background

Ganoderma lucidum is a basidiomycete fungus with a large number of hydrolytic enzymes in its genome capable of degrading cellulose. The efficiency of cellulose utilization is a determinant of its growth rate and fruiting body development. Understanding the molecular mechanisms regulating cellulose degradation is important for biomass conversion and sustainable energy utilization.

Objective

To identify and characterize the molecular mechanism by which the mitogen-activated protein kinase GlSlt2 regulates cellulase activity and cellulose utilization in Ganoderma lucidum through its interaction with the MYB transcription factor GlMyb.

Results

GlSlt2 positively modulates cellulase activity and cellulose utilization by phosphorylating GlMyb at the S245 site. GlMyb directly binds to the [A/G]TTAC[G/C][C/G] motif on promoters of cellulase-related genes (CBH1, CBH3, EG1, EG3, and EG5). Phosphorylation of S245 enhances GlMyb’s binding ability to these promoters and positively regulates cellulase gene expression.

Conclusion

This study reveals a sophisticated regulatory mechanism where GlSlt2 positively regulates GlMyb-mediated cellulose utilization through phosphorylation at a specific serine residue. These findings provide insights into enhancing cellulose degradation efficiency, which has important implications for biomass conversion and sustainable bioenergy production.
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