PXD054433-1

PXD054433 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_04:57:24.553.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	2024-07-31 05:29:16	ID requested
⏵ 1	2024-10-14 04:57:24	announced
2	2024-10-22 07:01:46	announced	2024-10-22: Updated project metadata.

10.1128/MBIO.02704-24;

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

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/10/PXD054433

PRIDE project URI

• PRIDE
  1. PXD054433
     1. Label: PRIDE project
     2. Name: S-palmitoylation of MAP kinase is essential for fungal virulence