BAIT

ESA1

TAS1, NuA4 histone acetyltransferase complex catalytic subunit ESA1, KAT5, L000003952, YOR244W
Catalytic subunit of the histone acetyltransferase complex (NuA4); acetylates four conserved internal lysines of histone H4 N-terminal tail and can acetylate histone H2A; master regulator of cellular acetylation balance; required for cell cycle progression and transcriptional silencing at the rDNA locus and regulation of autophagy; human ortholog TIP60/KAT5 is implicated in cancer and other diseases
Saccharomyces cerevisiae (S288c)
PREY

CMD1

calmodulin, CaM, L000000365, YBR109C
Calmodulin; Ca++ binding protein that regulates Ca++ independent processes (mitosis, bud growth, actin organization, endocytosis, etc.) and Ca++ dependent processes (stress-activated pathways), targets include Nuf1p, Myo2p and calcineurin
Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.

Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Cote J, Figeys DA, Baetz K

Recent global proteomic and genomic studies have determined that lysine acetylation is a highly abundant posttranslational modification. The next challenge is connecting lysine acetyltransferases (KATs) to their cellular targets. We hypothesize that proteins that physically interact with KATs may not only predict the cellular function of the KATs but may be acetylation targets. We have developed a mass spectrometry-based method ... [more]

Proc. Natl. Acad. Sci. U.S.A. Apr. 23, 2013; 110(17);E1641-50 [Pubmed: 23572591]

Throughput

  • High Throughput

Additional Notes

  • identified by mChIP-KAT-MS assay, which consists of three steps: isolation of a lysine acetyltransferase (KAT) and its associated protein network from cells, enrichment of acetylated lysine residues within the network by an in vitro KAT reaction; and identification of the interacting proteins and acetylation sites by LC-MS/MS

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CMD1 ESA1
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.208BioGRID
1920864

Curated By

  • BioGRID