CRWN2 Antibody

CRWN2 in DNA Damage Response and Genome Stability

CRWN2 interacts with DDR machinery to maintain genomic integrity. Key findings include:

CRWN2 physically associates with RAD51D (a recombinase) and SNI1 (a DDR protein) to form nuclear bodies at double-strand breaks (DSBs) . These interactions enable liquid–liquid phase separation (LLPS), creating dynamic repair compartments .

Protein Interactions and Genetic Pathways

CRWN2 forms homo- and hetero-oligomers with other CRWN proteins and DDR factors:

Genetic studies show crwn1 crwn2 double mutants exhibit synthetic lethality, with impaired DDR and increased chromatin fragmentation .

Epigenetic Regulation and Tissue-Specific Roles

CRWN2 maintains H3K27me3 landscapes, influencing gene expression in endosperm and leaves:

In crwn1/2 mutants, defense-related genes are ectopically activated, linking CRWN2 to suppression of stress responses .

Methodologies for CRWN2 Detection

While specific CRWN2 antibodies are not documented, researchers use:

1. GFP tagging: CRWN2:GFP fusion proteins enable live-cell imaging and subcellular localization studies .

2. Immunostaining: Anti-GFP antibodies detect tagged CRWN2 in γ-H2AX foci or nuclear periphery .

3. Chromatin Isolation by RNA Purification (ChIRP): Identifies CRWN2-bound genomic regions (e.g., pericentromeric and PR1 promoter regions) .

Meiotic Roles and Chromatin Release

During meiosis, CRWN2 is degraded to enable chromatin release from the nuclear envelope (NE):

CRWN2’s degradation during prophase I is linked to SCF^RMF-dependent ubiquitination, ensuring proper chromatin reorganization .

Defense Signaling and Stress Responses

CRWN2 suppresses salicylic acid (SA)-dependent defense pathways. In crwn1/2 mutants:

• Pathogen response: Partial resistance to Pseudomonas syringae due to constitutive SA signaling .

• ROS production: Elevated reactive oxygen species (ROS), linking DDR to stress signaling .