PXD048216-1

PXD048216 is an original dataset announced via ProteomeXchange.

Title	S-palmitoylation of MAP kinase is essential for fungal virulence
Description	acylation also called S-palmitoylation is an important reversible protein post-translational modification in organisms. However, its function remains unknown in pathogenic fungi. Here, we found treatment of rice false fungus Ustilaginoidea virens with S-palmitoylation inhibitor 2-BP resulted in a significant decrease in fungal virulence and growth rate. Deletion of the S-acyltransferase proteins from U. virens indicated that two S-acyltransferases UvPfa3 and UvPfa4 were required for fungal virulence. Comprehensive identification of S-palmitoylation sites and proteins in U. virens revealed a total of 4089 S-palmitoylation sites were identified within 2192 proteins and S-palmitoylation proteins were involved in diverse biological processes. Interestingly, S-palmitoylation proteins were significantly enriched in mitogen-activated protein kinase (MAPK) pathway and MAP kinase UvSlt2 was confirmed to be a S-palmitoylation protein which was palmitoylated by UvPfa4. Mutations of S-palmitoylation sites in UvSlt2 resulted in significantly reduced fungal virulence and decreased kinase enzymatic activity and phosphorylation level. Molecular dynamics simulations demonstrated mutation of S-palmitoylation sites in UvSlt2 caused decreased hydrophobic solvent-accessible surface area, and thereby affected binding between the UvSlt2 enzyme and substrates. Taken together, S-palmitoylation promotes U. virens virulence through palmitoylating MAP kinase UvSlt2 by palmitoyltransferase UvPfa4 and enhancing enzymatic activity and phosphorylation level of the kinase, thereby increasing hydrophobic solvent-accessible surface area and binding activity between the UvSlt2 enzyme and its substrates. Our studies provide a framework for dissecting the biological functions of S-palmitoylation, and reveal an important role for S-palmitoylation in regulating virulence of pathogen.
HostingRepository	PRIDE
AnnounceDate	2024-10-14
AnnouncementXML	Submission_2024-10-14_04:53:50.439.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	duan yuhang
SpeciesList	scientific name: Ustilaginoidea virens; NCBI TaxID: 1159556;
ModificationList	S-palmitoyl-L-cysteine
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2024-01-02 21:35:53	ID requested
⏵ 1	2024-10-14 04:53:50	announced
2	2024-10-22 07:01:46	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: S-palmitoylation

Biotin

Ustilaginoidea virens

virulence

Yuhang Duan
contact affiliation	College of Plant Science and Technology, Huazhong Agricultural University
contact email	281102634@qq.com
lab head
duan yuhang
contact affiliation	Huazhong Agricultural University
contact email	281102634@qq.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD048216
     1. Label: PRIDE project
     2. Name: S-palmitoylation of MAP kinase is essential for fungal virulence