BAIT

TTI2

YJR136C
Subunit of the ASTRA complex, involved in chromatin remodeling; telomere length regulator involved in the stability or biogenesis of PIKKs such as TORC1; similar to S. pombe Tti2p; may interact with Rsm23p; GFP-fusion protein localizes to the cytoplasm
GO Process (0)
GO Function (0)
GO Component (2)

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

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)

Dosage Lethality

A genetic interaction is inferred when over expression or increased dosage of one gene causes lethality in a strain that is mutated or deleted for another gene.

Publication

Saccharomyces cerevisiae Tti2 Regulates PIKK Proteins and Stress Response.

Hoffman KS, Duennwald ML, Karagiannis J, Genereaux J, McCarton AS, Brandl CJ

The TTT complex is composed of the three essential proteins Tel2, Tti1, and Tti2 The complex is required to maintain steady state levels of phosphatidylinositol 3-kinase-related kinase (PIKK) proteins, including mTOR, ATM/Tel1, ATR/Mec1, and TRRAP/Tra1, all of which serve as regulators of critical cell signaling pathways. Due to their association with heat shock proteins, and with newly synthesized PIKK peptides, ... [more]

G3 (Bethesda) Jun. 01, 2016; 6(6);1649-59 [Pubmed: 27172216]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • Overexpressing Hsp90 chaperones and cochaperones is lethal when Tti2 is depleted

Curated By

  • BioGRID