BAIT

RPP8

DISEASE RESISTANCE PROTEIN RPP8, HRT, HYPERSENSITIVE RESPONSE TO TCV, MWF20.19, MWF20_19, RCY1, RECOGNITION OF PERONOSPORA PARASITICA 8, RESISTANT TO CMV(Y) 1, AT5G43470
disease resistance protein RPP8
GO Process (5)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

CRT1A

AtCRT1a, CALRETICULIN 1, CRT1, F14G9.5, F14G9_5, calreticulin 1a, AT1G56340
calreticulin-1
GO Process (4)
GO Function (1)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)

PCA

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

SAG101 Forms a Ternary Complex with EDS1 and PAD4 and Is Required for Resistance Signaling against Turnip Crinkle Virus.

Zhu S, Jeong RD, Venugopal SC, Lapchyk L, Navarre D, Kachroo A, Kachroo P

EDS1, PAD4, and SAG101 are common regulators of plant immunity against many pathogens. EDS1 interacts with both PAD4 and SAG101 but direct interaction between PAD4 and SAG101 has not been detected, leading to the suggestion that the EDS1-PAD4 and EDS1-SAG101 complexes are distinct. We show that EDS1, PAD4, and SAG101 are present in a single complex in planta. While this ... [more]

PLoS Pathog. Nov. 01, 2011; 7(11);e1002318 [Pubmed: 22072959]

Throughput

  • Low Throughput

Curated By

  • BioGRID