BAIT

AT5G21990

tetratricopeptide repeat domain-containing protein OEP61
GO Process (3)
GO Function (2)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

ATERDJ2A

F19K16.10, F19K16_10, AT1G79940
J domain protein ATERDJ2A
GO Process (1)
GO Function (0)
GO Component (6)

Gene Ontology Biological Process

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

AtTPR7 is a chaperone docking protein of the Sec translocon in Arabidopsis.

Schweiger R, Mueller NC, Schmitt MJ, Soll J, Schwenkert S

Chaperone assisted sorting of post-translationally imported proteins is a general mechanism among all eukaryotic organisms. Interaction of some preproteins with the organellar membranes is mediated by chaperones, which are recognized by membrane bound tetratricopeptide repeat (TPR) domain containing proteins. We have characterized AtTPR7 as an endoplasmic reticulum (ER) protein in plants and propose a potential function for AtTPR7 in post-translational ... [more]

J. Cell. Sci. Aug. 16, 2012; 0(0); [Pubmed: 22899711]

Throughput

  • Low Throughput

Curated By

  • BioGRID