PXD046004 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Phosphorylation Promotes DELLA Activity by Enhancing Its Binding to Histone H2A at Target Chromatin in Arabidopsis |
Description | DELLA proteins are conserved master growth regulators that play a central role in controlling plant development in response to internal and environmental cues. DELLAs function as transcription regulators, which are recruited to target promoters by binding to transcription factors (TFs) and histone H2A via its GRAS domain. Recent studies showed that DELLA stability is regulated post-translationally via two mechanisms, phytohormone gibberellin-induced polyubiquitination for its rapid degradation, and Small Ubiquitin-like Modifier (SUMO)-conjugation to alter its accumulation. Moreover, DELLA activity is dynamically modulated by two distinct glycosylations: DELLA-TF interactions are enhanced by O-fucosylation, but inhibited by O-linked N-acetylglucosamine (O-GlcNAc) modification. However, the role of DELLA phosphorylation remains unclear. Here, we identified phosphorylation sites in REPRESSOR OF ga1-3 (RGA, an AtDELLA) purified from Arabidopsis by tandem mass spectrometry analysis, and showed that phosphorylation of the RGA LKS-peptide in the poly-S/T region enhances RGA-H2A interaction and RGA association with target promoters. Interestingly, phosphorylation does not affect RGA-TF interactions. Our study has uncovered that phosphorylation is a new regulatory mechanism of DELLA activity. |
HostingRepository | PRIDE |
AnnounceDate | 2024-08-08 |
AnnouncementXML | Submission_2024-08-08_10:13:05.955.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD046004 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Jeffrey Shabanowitz |
SpeciesList | scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; |
ModificationList | N-acetylhexosaminylated residue; fucosylated residue; phosphorylated residue; monohydroxylated residue; hexosylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-10-09 15:27:27 | ID requested | |
⏵ 1 | 2024-08-08 10:13:06 | announced | |
Publication List
Keyword List
submitter keyword: RGA phosphorylation,Arabidopsis, DELLA |
Contact List
Jeffrey Shabanowitz |
contact affiliation | Department of Chemistry,University of Virginia,Charlottesville, VA 22903 USA |
contact email | js4c@virginia.edu |
lab head | |
Jeffrey Shabanowitz |
contact affiliation | University of Virginia |
contact email | js4c@virginia.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD046004
- Label: PRIDE project
- Name: Phosphorylation Promotes DELLA Activity by Enhancing Its Binding to Histone H2A at Target Chromatin in Arabidopsis