BAIT

EAF1

VID21, YDR359C
Component of the NuA4 histone acetyltransferase complex; acts as a platform for assembly of NuA4 subunits into the native complex; required for initiation of pre-meiotic DNA replication, likely due to its requirement for expression of IME1
GO Process (3)
GO Function (0)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

ALG7

TUR1, UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase, L000000078, YBR243C
UDP-N-acetyl-glucosamine-1-P transferase; transfers Glc-Nac-P from UDP-GlcNac to Dol-P in the ER in the first step of the dolichol pathway of protein asparagine-linked glycosylation; inhibited by tunicamycin
GO Process (2)
GO Function (1)
GO Component (2)
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

Regulation of Septin Dynamics by the Saccharomyces cerevisiae Lysine Acetyltransferase NuA4.

Mitchell L, Lau A, Lambert JP, Zhou H, Fong Y, Couture JF, Figeys D, Baetz K

In the budding yeast Saccharomyces cerevisiae, the lysine acetyltransferase NuA4 has been linked to a host of cellular processes through the acetylation of histone and non-histone targets. To discover proteins regulated by NuA4-dependent acetylation, we performed genome-wide synthetic dosage lethal screens to identify genes whose overexpression is toxic to non-essential NuA4 deletion mutants. The resulting genetic network identified a novel ... [more]

PLoS ONE Oct. 11, 2011; 6(10);e25336 [Pubmed: 21984913]

Throughput

  • High Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • determined by SGA
  • overexpression in an eaf1 mutant background is lethal

Curated By

  • BioGRID