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

GLO2

hydroxyacylglutathione hydrolase GLO2, L000003488, YDR272W
Cytoplasmic glyoxalase II; catalyzes the hydrolysis of S-D-lactoylglutathione into glutathione and D-lactate; GLO2 has a paralog, GLO4, that arose from the whole genome duplication
GO Process (1)
GO Function (1)
GO Component (1)

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.

Bertgen L, Boekenkamp JE, Schneckmann T, Koch C, Raeschle M, Storchova Z, Herrmann JM

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