BAIT

TOC64-V

ARABIDOPSIS THALIANA TRANSLOCON AT THE OUTER MEMBRANE OF CHLOROPLASTS 64-V, ATTOC64-V, MTOM64, T5E8.220, T5E8_220, translocon at the outer membrane of chloroplasts 64-V, AT5G09420
translocon at the outer membrane of chloroplasts 64-V
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

HSP81-2

AtHsp90.2, EARLY-RESPONSIVE TO DEHYDRATION 8, ERD8, HEAT SHOCK PROTEIN 81-2, HEAT SHOCK PROTEIN 90.2, HSP90.2, MDA7.7, MDA7_7, AT5G56030
heat shock protein 81-2
Arabidopsis thaliana (Columbia)

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.

Publication

Quantification of interaction strengths between chaperones and tetratricopeptide repeat domain containing membrane proteins.

Schweiger R, Soll J, Jung K, Heermann R, Schwenkert S

The three tetratricopeptide repeat domain containing docking proteins Toc64, OM64 and AtTPR7 reside in the chloroplast, mitochondria and endoplasmic reticulum of Arabidopsis thaliana, respectively. They are suggested to act during post-translational protein import by association with chaperone bound preprotein complexes. Here we performed a detailed biochemical, biophysical and computational analysis of the interaction between Toc64, OM64 and AtTPR7 and the ... [more]

J. Biol. Chem. Sep. 13, 2013; 0(0); [Pubmed: 24036116]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TOC64-V HSP81-2
Reconstituted Complex
Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Low-BioGRID
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Curated By

  • BioGRID