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
Saccharomyces cerevisiae (S288c)
PREY

RSM24

mitochondrial 37S ribosomal protein RSM24, YDR175C
Mitochondrial ribosomal protein of the small subunit
GO Process (1)
GO Function (1)
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

MitoStores: chaperone-controlled protein granules store mitochondrial precursors in the cytosol.

Kraemer L, Dalheimer N, Raeschle M, Storchova Z, Pielage J, Boos F, Herrmann JM

Hundreds of nucleus-encoded mitochondrial precursor proteins are synthesized in the cytosol and imported into mitochondria in a post-translational manner. However, the early processes associated with mitochondrial protein targeting remain poorly understood. Here, we show that in Saccharomyces cerevisiae, the cytosol has the capacity to transiently store mitochondrial matrix-destined precursors in dedicated deposits that we termed MitoStores. Competitive inhibition of mitochondrial ... [more]

EMBO J Apr. 03, 2023; 42(7);e112309 [Pubmed: 36704946]

Throughput

  • High Throughput

Curated By

  • BioGRID