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
GO Process (7)
GO Function (2)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
SIR2
MAR1, NAD-dependent histone deacetylase SIR2, L000001895, YDL042C
Conserved NAD+ dependent histone deacetylase of the Sirtuin family; involved in regulation of lifespan; plays roles in silencing at HML, HMR, telomeres, and the rDNA locus; negatively regulates initiation of DNA replication; functions as a regulator of autophagy like mammalian homolog SIRT1, and also of mitophagy; SIR2 has a paralog, HST1, that arose from the whole genome duplication
GO Process (8)
GO Function (5)
GO Component (6)
Gene Ontology Biological Process
- chromatin assembly or disassembly [IDA]
- chromatin silencing at rDNA [IMP]
- chromatin silencing at silent mating-type cassette [IMP]
- chromatin silencing at telomere [IMP]
- chronological cell aging [IMP]
- negative regulation of DNA recombination [IGI]
- negative regulation of DNA replication [IMP]
- replicative cell aging [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).
The Hsp90 chaperone cycle catalyzes the final activation step of several important eukaryotic proteins (Hsp90 "clients"). Although largely a functional form of Hsp90, an Hsp90-Gal4p DNA binding domain fusion (Hsp90-BD) displays no strong interactions in the yeast two-hybrid system, consistent with a general transience of most Hsp90-client associations. Strong in vivo interactions are though detected when the E33A mutation is ... [more]
Eukaryotic Cell May. 01, 2005; 4(5);849-60 [Pubmed: 15879519]
Throughput
- High Throughput
Curated By
- BioGRID