PXD029477 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Cavity surface residues of PAD4 and SAG101 contribute to EDS1 dimer signaling specificity in plant immunity |
Description | Arabidopsis pathogen effector-triggered immunity (ETI) is controlled by a family of three lipase-like proteins EDS1, PAD4 and SAG101 and two sub-families of HET-S/LOB-B (HeLo)-domain “helper” NLRs, ADR1s and NRG1s. EDS1-PAD4 dimers cooperate with ADR1s, and EDS1-SAG101 dimers with NRG1s, in two separate defense-promoting modules. EDS1-PAD4-ADR1 and EDS1- SAG101-NRG1 complexes were detected in immune-activated leaf extracts but the molecular determinants for specific complex formation and function remain unknown. EDS1 signaling is mediated by a C-terminal EP domain (EPD) surface surrounding a cavity formed by the heterodimer. Here we investigated whether the EPDs of PAD4 and SAG101 contribute to EDS1 dimer functions. Using a structure-guided approach, we undertook a comprehensive mutational analysis of Arabidopsis PAD4. We identify two conserved residues (Arg314 and Lys380) lining the PAD4 EPD cavity that are essential for EDS1-PAD4 mediated pathogen resistance, but are dispensible for PAD4 mediated restriction of green peach aphid infestation. Positionally equivalent Met304 and Arg373 at the SAG101 EPD cavity are required for EDS1-SAG101 promotion of ETI-related cell death. In a PAD4 and SAG101 interactome analysis of ETI-activated tissues, PAD4R314A and SAG101M304R EPD variants maintain interaction with EDS1 but lose association, respectively, with helper NLRs ADR1-L1 and NRG1.1, and other immune-related proteins. Our data reveal a fundamental contribution of similar but non-identical PAD4 and SAG101 EPD surfaces to specific EDS1 dimer protein interactions and pathogen immunity. |
HostingRepository | PRIDE |
AnnounceDate | 2022-03-17 |
AnnouncementXML | Submission_2022-03-17_09:30:26.968.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Sara Christina Stolze |
SpeciesList | scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; |
ModificationList | No PTMs are included in the dataset |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-11-01 07:01:12 | ID requested | |
⏵ 1 | 2022-03-17 09:30:27 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: NLR, EDS1, PAD4, SAG101, ETI, immunity, plant |
Contact List
Hirofumi Nakagami |
contact affiliation | Basic Immune System of Plants / Protein Mass Spectrometry Max Planck Institute for Plant Breeding Research Carl-von-Linne-Weg 10, 50829 Cologne, Germany |
contact email | nakagami@mpipz.mpg.de |
lab head | |
Sara Christina Stolze |
contact affiliation | Plant Proteomics and Mass Spectrometry Group Max Planck Institute for Plant Breeding Research Carl-von-Linné Weg 10 50829 Cologne |
contact email | stolze@mpipz.mpg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD029477
- Label: PRIDE project
- Name: Cavity surface residues of PAD4 and SAG101 contribute to EDS1 dimer signaling specificity in plant immunity