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)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
PDR5
LEM1, STS1, YDR1, ATP-binding cassette multidrug transporter PDR5, L000001365, L000002136, L000002504, YOR153W
Plasma membrane ATP-binding cassette (ABC) transporter; multidrug transporter actively regulated by Pdr1p; also involved in steroid transport, cation resistance, and cellular detoxification during exponential growth; PDR5 has a paralog, PDR15, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Distinct types of intramitochondrial protein aggregates protect mitochondria against proteotoxic stress.
Mitochondria consist of hundreds of proteins, most of which are inaccessible to the proteasomal quality control system of the cytosol. How cells stabilize the mitochondrial proteome during challenging conditions remains poorly understood. Here, we show that mitochondria form spatially defined protein aggregates as a stress-protecting mechanism. Two different types of intramitochondrial protein aggregates can be distinguished. The mitoribosomal protein Var1 ... [more]
Cell Rep Apr. 23, 2024; 43(4);114018 [Pubmed: 38551959]
Throughput
- High Throughput
Additional Notes
- in rho0 background
Curated By
- BioGRID