BAIT

DNMT2

AtDNMT2, DNA METHYLTRANSFERASE 2, DNA methyltransferase-2, T14C9.10, T14C9_10, AT5G25480
DNA methyltransferase-2
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

HD2B

ARABIDOPSIS HISTONE DEACETYLASE 2, ATHD2, ATHD2B, HD2, HDA4, HDT02, HDT2, HISTONE DEACETYLASE, HISTONE DEACETYLASE 2, MDJ22.7, MDJ22_7, histone deacetylase 2B, AT5G22650
histone deacetylase HDT2
Arabidopsis thaliana (Columbia)

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Arabidopsis DNA methyltransferase AtDNMT2 associates with histone deacetylase AtHD2s activity.

Song Y, Wu K, Dhaubhadel S, An L, Tian L

DNA methyltransferase2 (DNMT2) is always deemed to be enigmatic, because it contains highly conserved DNA methyltransferase motifs but lacks the DNA methylation catalytic capability. Here we show that Arabidopsis DNA methyltransferase2 (AtDNMT2) is localized in nucleus and associates with histone deacetylation. Bimolecular fluorescence complementation and pull-down assays show AtDNMT2 interacts with type-2 histone deacetylases (AtHD2s), a unique type of histone ... [more]

Biochem. Biophys. Res. Commun. May. 28, 2010; 396(2);187-92 [Pubmed: 20331964]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
DNMT2 HD2B
PCA
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.

Low-BioGRID
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Curated By

  • BioGRID