BAIT

AT4G25370

T30C3.40, T30C3_40
Double Clp-N motif protein
GO Process (0)
GO Function (1)
GO Component (5)

Gene Ontology Molecular Function

Arabidopsis thaliana (Columbia)
PREY

HSP93-III

ATCLPC, ATHSP93-III, AT3G48870
Clp ATPase
Arabidopsis thaliana (Columbia)

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.

Publication

Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones.

Colombo CV, Ceccarelli EA, Rosano GL

The caseinolytic protease (Clp) is crucial for chloroplast biogenesis and proteostasis. The Arabidopsis Clp consists of two heptameric rings (P and R rings) assembled from nine distinct subunits. Hsp100 chaperones (ClpC1/2 and ClpD) are believed to dock to the axial pores of Clp and then transfer unfolded polypeptides destined to degradation. The adaptor proteins ClpT1 and 2 attach to the ... [more]

BMC Plant Biol. Aug. 26, 2014; 14(0);228 [Pubmed: 25149061]

Throughput

  • Low Throughput

Curated By

  • BioGRID