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

Analysis of functions of VIP1 and its close homologs in osmosensory responses of Arabidopsis thaliana.

Tsugama D, Liu S, Takano T

VIP1 is a bZIP protein in Arabidopsis thaliana. VIP1 accumulates in the nucleus under hypo-osmotic conditions and interacts with the promoters of hypo-osmolarity-responsive genes, CYP707A1 and CYP707A3 (CYP707A1/3), but neither overexpression of VIP1 nor truncation of its DNA-binding region affects the expression of CYP707A3 in vivo, raising the possibility that VIP and other proteins are functionally redundant. Here we show ... [more]

PLoS ONE Aug. 06, 2014; 9(8);e103930 [Pubmed: 25093810]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
VIP1 AT2G31370	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.	Tsugama D (2014)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

VIP1

Gene Ontology Biological Process

Gene Ontology Molecular Function

mitogen-activated protein kinase binding [IPI]protein binding [IPI]sequence-specific DNA binding [IDA]sequence-specific DNA binding transcription factor activity [IDA, ISS]

Gene Ontology Cellular Component

AT2G31370