BAIT
HSP104
chaperone ATPase HSP104, L000000823, YLL026W
Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation
GO Process (7)
GO Function (5)
GO Component (3)
Gene Ontology Biological Process
- cellular heat acclimation [IMP]
- chaperone cofactor-dependent protein refolding [IDA]
- inheritance of oxidatively modified proteins involved in replicative cell aging [IGI, IMP]
- protein folding in endoplasmic reticulum [IMP]
- protein unfolding [IMP]
- stress granule disassembly [IDA]
- trehalose metabolism in response to heat stress [IMP]
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
RPS13
RPS13B, RPS13C, ribosomal 40S subunit protein S13, YS15, S27a, S15, S13, L000002900, L000002655, YDR064W
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S13 and bacterial S15
GO Process (2)
GO Function (2)
GO Component (2)
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
Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.
The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. ... [more]
Nat Commun Jan. 05, 2024; 15(1);315 [Pubmed: 38182580]
Throughput
- Low Throughput
Curated By
- BioGRID