BAIT

PIH1

NOP17, YHR034C
Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly large protein complexes such as box C/D snoRNPs and RNA polymerase II
GO Process (4)
GO Function (0)
GO Component (4)
Saccharomyces cerevisiae (S288c)
PREY

KRE28

YDR532C
Subunit of a kinetochore-microtubule binding complex; complex bridges centromeric heterochromatin and kinetochore MAPs and motors; required for sister chromatid bi-orientation and kinetochore binding of SAC components; complex also includes Spc105p; modified by sumoylation
GO Process (0)
GO Function (0)
GO Component (3)
Saccharomyces cerevisiae (S288c)

Synthetic Growth Defect

A genetic interaction is inferred when mutations in separate genes, each of which alone causes a minimal phenotype, result in a significant growth defect under a given condition when combined in the same cell.

Publication

Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation.

Zhao R, Kakihara Y, Gribun A, Huen J, Yang G, Khanna M, Costanzo M, Brost RL, Boone C, Hughes TR, Yip CM, Houry WA

Hsp90 is a highly conserved molecular chaperone that is involved in modulating a multitude of cellular processes. In this study, we identify a function for the chaperone in RNA processing and maintenance. This functionality of Hsp90 involves two recently identified interactors of the chaperone: Tah1 and Pih1/Nop17. Tah1 is a small protein containing tetratricopeptide repeats, whereas Pih1 is found to ... [more]

J. Cell Biol. Feb. 11, 2008; 180(3);563-78 [Pubmed: 18268103]

Throughput

  • High Throughput

Ontology Terms

  • phenotype: vegetative growth (APO:0000106)

Additional Notes

  • HTP: SGA

Curated By

  • BioGRID