BAIT

HSP82

HSP90, Hsp90 family chaperone HSP82, L000000822, YPL240C
Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

GIS2

L000004862, YNL255C
Translational activator for mRNAs with internal ribosome entry sites; associates with polysomes and binds to a specific subset of mRNAs; localizes to RNA processing bodies (P bodies) and to stress granules; may have a role in translation regulation under stress conditions; ortholog of human ZNF9/CNBP, a gene involved in myotonic dystrophy type 2
GO Process (1)
GO Function (3)
GO Component (4)
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

The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range.

Girstmair H, Tippel F, Lopez A, Tych K, Stein F, Haberkant P, Schmid PWN, Helm D, Rief M, Sattler M, Buchner J

The molecular chaperone Hsp90 is an important regulator of proteostasis. It has remained unclear why S. cerevisiae possesses two Hsp90 isoforms, the constitutively expressed Hsc82 and the stress-inducible Hsp82. Here, we report distinct differences despite a sequence identity of 97%. Consistent with its function under stress conditions, Hsp82 is more stable and refolds more efficiently than Hsc82. The two isoforms ... [more]

Nat Commun Aug. 09, 2019; 10(1);3626 [Pubmed: 31399574]

Throughput

  • High Throughput

Additional Notes

  • heatshock

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
GIS2 HSP82
Affinity Capture-RNA
Affinity Capture-RNA

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and associated RNA species identified by Northern blot, RT-PCR, affinity labeling, sequencing, or microarray analysis.

High-BioGRID
-
HSP82 GIS2
Synthetic Lethality
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.

High-BioGRID
167151

Curated By

  • BioGRID