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GlPRMT5 inhibits GlPP2C1 via symmetric dimethylation and regulates the biosynthesis of secondary metabolites in Ganoderma lucidum

ABSTRACT: After incubating the purified pColdI-PRMT5, pColdI-PP2C1 and SAM in the above 50 μL reaction buffer, they were treated at 30 °C for 90 minutes and separated on a 12% (wt/vol) SDS‒PAGE gel. The GlPP2C1 protein was cleaved, digested with trypsin in the gel, and analyzed by LC‒MS/MS analysis of polypeptides. Peptide identification was performed using MS/MS spectra of the GlPP2C1 protein.

INSTRUMENT(S):

ORGANISM(S): Ganoderma Lucidum

SUBMITTER: Zi Wang

LAB HEAD: Zi Wang

PROVIDER: PXD048799 | Pride | 2024-02-15

REPOSITORIES: Pride

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			Action	DRS
	480_FPEP220076007-1A.raw	Raw
	480_FPEP220076007-1A_PeptideGroups.xls	Xls
	480_FPEP220076007-1A_Proteins.xls	Xls
	checksum.txt	Txt
	mqpar.xml	Xml

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GlPRMT5 inhibits GlPP2C1 via symmetric dimethylation and regulates the biosynthesis of secondary metabolites in Ganoderma lucidum.

Project description:PRMT5, a type II arginine methyltransferase, is involved in transcriptional regulation, RNA processing and other biological processes and signal transduction. Secondary metabolites are vital pharmacological compounds in Ganoderma lucidum, and their content is an important indicator for evaluating the quality of G. lucidum. Here, we found that GlPRMT5 negatively regulates the biosynthesis of secondary metabolites. In further in-depth research, GlPP2C1 (a type 2C protein phosphatase) was identified out as an interacting protein of GlPRMT5 by immunoprecipitation-mass spectrometry (IP-MS). Further mass spectrometry detection revealed that GlPRMT5 symmetrically dimethylates the arginine 99 (R99) and arginine 493 (R493) residues of GlPP2C1 to weaken its activity. The symmetrical dimethylation modification of the R99 residue is the key to affecting GlPP2C1 activity. Symmetrical demethylation-modified GlPP2C1 does not affect the interaction with GlPRMT5. In addition, silencing GlPP2C1 clearly reduced GA content, indicating that GlPP2C1 positively regulates the biosynthesis of secondary metabolites in G. lucidum. In summary, this study reveals the molecular mechanism by which GlPRMT5 regulates secondary metabolites, and these studies provide further insights into the target proteins of GlPRMT5 and symmetric dimethylation sites. Furthermore, these studies provide a basis for the mutual regulation between different epigenetic modifications.

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