BAIT
HSP90
CaO6.7645, CAWG_05553, CaJ7_0234, IPF4596.2, Contig4-3089_0026, IPF20556.1, C7_02030W_B, orf19.13868, orf19_6515, CaO19.6515, CaO19_6515, orf6.7645, CaO19.13868, CA4959, C7_02030W, orf19.6515, CaJ7.0234, C7_02030W_A
Essential chaperone, regulates several signal transduction pathways and temperature-induced morphogenesis; activated by heat shock, stress; localizes to surface of hyphae, not yeast cells; mediates echinocandin and biofilm azole resistance
GO Process (0)
GO Function (0)
GO Component (0)
Candida albicans (SC5314)
PREY
SIK1
Contig4-3105_0047, IPF929.2, CaO6.8917, orf19.7569, CR_09950C, CA5975, CAWG_02259, CaO19.7569, CR_09950C_B, orf6.8917, CR_09950C_A
Putative U3 snoRNP protein; Hap43p-induced gene; physically interacts with TAP-tagged Nop1p
GO Process (0)
GO Function (0)
GO Component (0)
Candida albicans (SC5314)
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
Global proteomic analyses define an environmentally contingent Hsp90 interactome and reveal chaperone-dependent regulation of stress granule proteins and the R2TP complex in a fungal pathogen.
Hsp90 is a conserved molecular chaperone that assists in the folding and function of diverse cellular regulators, with a profound impact on biology, disease, and evolution. As a central hub of protein interaction networks, Hsp90 engages with hundreds of protein-protein interactions within eukaryotic cells. These interactions include client proteins, which physically interact with Hsp90 and depend on the chaperone for ... [more]
PLoS Biol. Jul. 08, 2019; 17(7);e3000358 [Pubmed: 31283755]
Throughput
- High Throughput
Additional Notes
- Affinity capture-MS under basal conditions (Table S1)
- Used Hsp90 E36A mutant which traps interacting proteins by decreasing Hsp90 ATPase activity
Curated By
- BioGRID