BAIT

HSC82

HSP90, Hsp90 family chaperone HSC82, L000000813, YMR186W
Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

TRE2

YOR256C
Transferrin receptor-like protein; functions with Tre1p to regulate ubiquitylation and vacuolar degradation of the metal transporter Smf1p; inviability of null mutant in systematic studies is due to proximity to CDC31; TRE2 has a paralog, TRE1, that arose from the whole genome duplication
UPS Project
Saccharomyces cerevisiae (S288c)

Synthetic Growth Defect

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

Publication

Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches.

McClellan AJ, Xia Y, Deutschbauer AM, Davis RW, Gerstein M, Frydman J

A comprehensive understanding of the cellular functions of the Hsp90 molecular chaperone has remained elusive. Although Hsp90 is essential, highly abundant under normal conditions, and further induced by environmental stress, only a limited number of Hsp90 "clients" have been identified. To define Hsp90 function, a panel of genome-wide chemical-genetic screens in Saccharomyces cerevisiae were combined with bioinformatic analyses. This approach ... [more]

Cell Oct. 05, 2007; 131(1);121-35 [Pubmed: 17923092]

Throughput

  • High Throughput

Ontology Terms

  • phenotype: vegetative growth (APO:0000106)

Additional Notes

  • A genome-wide chemical-genetic screen was used to identify deletion strains whose growth was negatively affected when Hsp90 function was compromised using the HSP90-inhibiting drug, macbecin II.

Curated By

  • BioGRID