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

EDL3 is an F-box protein involved in the regulation of abscisic acid signalling in Arabidopsis thaliana.

Koops P, Pelser S, Ignatz M, Klose C, Marrocco-Selden K, Kretsch T

The EID1-like protein 3 (EDL3) shows high similarity to EID1 (Empfindlicher im dunkelroten Licht 1), an F-box protein that functions as a negative regulator in the signalling cascade downstream of the phytochrome A photoreceptor in Arabidopsis thaliana. Analyses revealed a strong and rapid induction of EDL3 gene expression under osmotic stress, high salinity, and upon abscisic acid (ABA) application. Therefore, ... [more]

Unknown Aug. 09, 2011; 0(0); [Pubmed: 21831845]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
SK18 EDL3	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.	Braun P (2011)	High	-	BioGRID	-
EDL3 SK18	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.	Koops P (2011)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

EDL3

Gene Ontology Biological Process

Gene Ontology Cellular Component

SK18

Gene Ontology Molecular Function

protein binding [IPI]ubiquitin-protein transferase activity [ISS]