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 acyl-CoA-binding protein ACBP1 participates in the regulation of seed germination and seedling development.

Du ZY, Chen MX, Chen QF, Xiao S, Chye ML

A family of six genes encoding acyl-CoA-binding proteins (ACBPs), ACBP1-ACBP6, has been characterized in Arabidopsis thaliana. In this study, we demonstrate that ACBP1 promotes abscisic acid (ABA) signaling during germination and seedling development. ACBP1 was induced by ABA, and transgenic Arabidopsis ACBP1-over-expressors showed increased sensitivity to ABA during germination and seedling development, whereas the acbp1 mutant showed decreased ABA sensitivity ... [more]

Plant J. Mar. 01, 2013; 0(0); [Pubmed: 23448237]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
ACBP1 PLDALPHA1	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.	Du ZY (2013)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

ACBP1

Gene Ontology Biological Process

Gene Ontology Molecular Function

fatty-acyl-CoA binding [IDA]lead ion binding [IDA]lipid binding [IDA]phosphatidic acid binding [IDA]protein binding [IPI]

Gene Ontology Cellular Component

PLDALPHA1