PXD046004

PXD046004 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2023-10-09 15:27:27	ID requested
⏵ 1	2024-08-08 10:13:06	announced

10.6019/PXD046004;

submitter keyword: RGA phosphorylation,Arabidopsis, DELLA

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

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PRIDE project URI

• PRIDE
  1. PXD046004
     1. Label: PRIDE project
     2. Name: Phosphorylation Promotes DELLA Activity by Enhancing Its Binding to Histone H2A at Target Chromatin in Arabidopsis