PREY

CCT7

TCP7, L000002763, YJL111W
Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo; mutant has increased aneuploidy tolerance
GO Process (1)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Publication

A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.

Reissmann S, Joachimiak LA, Chen B, Meyer AS, Nguyen A, Frydman J

The eukaryotic chaperonin TRiC/CCT uses ATP cycling to fold many essential proteins that other chaperones cannot fold. This 1 MDa hetero-oligomer consists of two identical stacked rings assembled from eight paralogous subunits, each containing a conserved ATP-binding domain. Here, we report a dramatic asymmetry in the ATP utilization cycle of this ring-shaped chaperonin, despite its apparently symmetric architecture. Only four of ... [more]

Cell Rep Oct. 25, 2012; 2(4);866-77 [Pubmed: 23041314]

Throughput

  • Low Throughput

Additional Notes

  • Figure 5

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CCT7 ACT1
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.226BioGRID
1939458

Curated By

  • BioGRID