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.

Publication

TRANSPARENT TESTA1 interacts with R2R3-MYB factors and affects early and late steps of flavonoid biosynthesis in the endothelium of Arabidopsis thaliana seeds.

Appelhagen I, Lu GH, Huep G, Schmelzer E, Weisshaar B, Sagasser M

Wild type seed coats of Arabidopsis thaliana are brown due to the accumulation of proanthocyanidin pigments (PAs). The pigmentation requires activation of phenylpropanoid biosynthesis genes and mutations in some of these genes cause a yellow appearance of seeds, termed transparent testa (tt) phenotype. The TT1 gene encodes a WIP-type zinc finger protein and is expressed in the seed coat endothelium ... [more]

Unknown Apr. 07, 2011; 0(0); [Pubmed: 21477081]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
TT1 TT2	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.	Appelhagen I (2011)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

TT1

Gene Ontology Biological Process

Gene Ontology Molecular Function

sequence-specific DNA binding transcription factor activity [ISS, TAS]

Gene Ontology Cellular Component

TT2