Proteomics

Dataset Information

0

: Identification of interactors of Arabidopsis VIN3 wildtype and VIN3 chimeric mutant protein in vernalized seedlings


ABSTRACT: The Arabidopsis VEL proteins VIN3 and VRN5 are accessory proteins of the Polycomb Repressive Complex 2 (PRC2). Their function is most well-understood in the epigenetic PRC2-mediated silencing of the floral repressor gene Flowering Locus C (FLC) during prolonged cold (vernalization). To identify protein interactors of VIN3 and VIN3 chimeric mutant protein carrying VRN5VEL instead of VIN3VEL, we used stable Arabidopsis transgenic lines expressing VIN3-GFP WT and VIN3-GFP VRN5VEL under endogenous promoters to perform native co-immunoprecipitation assays in seedlings vernalized for six weeks at 5 °C. Non-transgenic Col-FRI was used as a negative control.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Seedling

SUBMITTER: Gerhard Saalbach  

LAB HEAD: Caroline Dean

PROVIDER: PXD064199 | Pride | 2025-08-28

REPOSITORIES: Pride

Dataset's files

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250318_01.mzML Mzml
250318_01.mzid Mzid
250318_01.raw Raw
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Publications

VEL-dependent polymerization maintains the chromatin association of Polycomb proteins for the switch to epigenetic silencing.

Schulten Anna A   Jang Geng-Jen GJ   Payne-Dwyer Alex A   Fiedler Marc M   Nielsen Mathias L ML   Mateo-Bonmatí Eduardo E   Bienz Mariann M   Leake Mark C MC   Dean Caroline C  

Molecular cell 20250825 17


Multivalent protein-chromatin interactions facilitated by higher-order protein assemblies are emerging as a crucial theme in eukaryotic gene regulation. However, understanding the underlying mechanisms in their functional context remains challenging. Arabidopsis VEL proteins assemble biomolecular condensates by head-to-tail polymerization. Here, we dissect the role of VEL polymerization domains in conferring the epigenetic switch to Polycomb repressive complex 2 (PRC2) silencing at Arabidopsis F  ...[more]

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