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

AHA1

YDR214W
Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress
GO Process (2)
GO Function (2)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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