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

Plastid division control: the PDV proteins regulate DRP5B dynamin activity.

Holtsmark I, Lee S, Lunde KA, Auestad K, Maple-Grodem J, Moller SG

Chloroplast division represents a fundamental but complex biological process involving remnants of the ancestral bacterial division machinery and proteins of eukaryotic origin. Moreover, the chloroplast division machinery is divided into stromal and cytosolic sub machineries, which coordinate and control their activities to ensure appropriate division initiation and progression. Dynamin related protein 5B (DRP5B) and plastid division protein 1 and 2 ... [more]

Plant Mol. Biol. Jun. 01, 2013; 82(3);255-66 [Pubmed: 23595201]

Throughput

Low Throughput

Additional Notes

Figure 3
bimolecular fluorescence complementation (BiFC)

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
PDV1 ARC5	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.	Holtsmark I (2013)	Low	-	BioGRID	1115352

Curated By

BioGRID

Interaction Summary

ARC5

Gene Ontology Biological Process

Gene Ontology Molecular Function

identical protein binding [IDA]protein binding [IPI]

Gene Ontology Cellular Component

PDV1