BAIT

HD1

ARABIDOPSIS HISTONE DEACETYLASE 1, ARABIDOPSIS HISTONE DEACETYLASE 19, ATHD1, ATHDA19, ATRPD3A, F20D10.250, F20D10_250, HDA1, HDA19, HISTONE DEACETYLASE, HISTONE DEACETYLASE 19, HISTONE DEACETYLASE19, RPD3A, histone deacetylase 1, AT4G38130
histone deacetylase 19
Arabidopsis thaliana (Columbia)
PREY

SNL1

SIN3-like 1, T22N4.5, T22N4_5, AT3G01320
paired amphipathic helix protein Sin3-like 1
GO Process (2)
GO Function (1)
GO Component (1)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)

PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

Publication

Arabidopsis Paired Amphipathic Helix Proteins SNL1 and SNL2 Redundantly Regulate Primary Seed Dormancy via Abscisic Acid-Ethylene Antagonism Mediated by Histone Deacetylation.

Wang Z, Cao H, Sun Y, Li X, Chen F, Carles A, Li Y, Ding M, Zhang C, Deng X, Soppe WJ, Liu YX

Histone (de)acetylation is a highly conserved chromatin modification that is vital for development and growth. In this study, we identified a role in seed dormancy for two members of the histone deacetylation complex in Arabidopsis thaliana, SIN3-LIKE1 (SNL1) and SNL2. The double mutant snl1 snl2 shows reduced dormancy and hypersensitivity to the histone deacetylase inhibitors trichostatin A and diallyl disulfide ... [more]

Plant Cell Jan. 31, 2013; 0(0); [Pubmed: 23371947]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HD1 SNL1
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Low-BioGRID
-

Curated By

  • BioGRID