BAIT

HSP78

chaperone ATPase HSP78, L000000821, YDR258C
Oligomeric mitochondrial matrix chaperone; cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates
GO Process (5)
GO Function (2)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

PET122

L000001397, YER153C
Mitochondrial translational activator specific for the COX3 mRNA; acts together with Pet54p and Pet494p; located in the mitochondrial inner membrane
Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

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 is identified by mass spectrometric methods.

Publication

Elucidation of the interaction proteome of mitochondrial chaperone Hsp78 highlights its role in protein aggregation during heat stress.

Jaworek W, Sylvester M, Cenini G, Voos W

Chaperones of the Hsp100/Clp family represent major components of protein homeostasis, conferring maintenance of protein activity under stress. The ClpB-type members of the family, present in bacteria, fungi, and plants, are able to resolubilize aggregated proteins. The mitochondrial member of the ClpB family in Saccharomyces cerevisiae is Hsp78. Although Hsp78 has been shown to contribute to proteostasis in elevated temperatures, ... [more]

J Biol Chem Oct. 01, 2022; 298(10);102494 [Pubmed: 36115461]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HSP78 PET122
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-0.1558BioGRID
2098340

Curated By

  • BioGRID