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

Negative feedback regulation of UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis.

Gruber H, Heijde M, Heller W, Albert A, Seidlitz HK, Ulm R

Plants respond to low levels of UV-B radiation with a coordinated photomorphogenic response that allows acclimation to this environmental stress factor. The key players in this UV-B response are COP1 (an E3 ubiquitin ligase), UVR8 (a Î²-propeller protein), and HY5 (a bZIP transcription factor). We have shown previously that an elevated UV-B-specific response is associated with dwarf growth, indicating the ... [more]

Unknown Nov. 01, 2010; 0(0); [Pubmed: 21041653]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
UVR8 AT5G23730	Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.	Heijde M (2013)	Low	-	BioGRID	-
AT5G23730 UVR8	Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Gruber H (2010)	Low	-	BioGRID	-
UVR8 AT5G23730	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.	Cloix C (2012)	Low	-	BioGRID	-
UVR8 AT5G23730	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.	Huang X (2014)	Low	-	BioGRID	-
UVR8 AT5G23730	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.	Yin R (2015)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

UVR8

Gene Ontology Biological Process

Gene Ontology Molecular Function

chromatin binding [IDA]guanyl-nucleotide exchange factor activity [ISS]protein binding [IPI]protein homodimerization activity [IDA]

Gene Ontology Cellular Component

AT5G23730