BAIT

YDJ1

HSP40, MAB3, MAS5, type I HSP40 co-chaperone YDJ1, L000002503, L000003567, S000029274, YNL064C
Type I HSP40 co-chaperone; involved in regulation of HSP90 and HSP70 functions; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; member of the DnaJ family
Saccharomyces cerevisiae (S288c)
PREY

SSA3

YG106, Hsp70 family ATPase SSA3, L000002071, L000000820, YBL075C
ATPase involved in protein folding and the response to stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; SSA3 has a paralog, SSA4, that arose from the whole genome duplication
GO Process (3)
GO Function (2)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Publication

Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo.

Becker J, Walter W, Yan W, Craig EA

In order to analyze the in vivo role of the SSA class of cytosolic 70-kDa heat shock proteins (hsps) of Saccharomyces cerevisiae, we isolated a temperature-sensitive mutant of SSA1. The effect of a shift of mutant cells (ssa1ts ssa2 ssa3 ssa4) from the permissive temperature of 23 degrees C to the nonpermissive temperature of 37 degrees C on the processing ... [more]

Mol. Cell. Biol. Aug. 01, 1996; 16(8);4378-86 [Pubmed: 8754838]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • in ydj1 ssa1 ssa2 ssa3 ssa4

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SSA3 YDJ1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
-

Curated By

  • BioGRID