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

HTZ1

HTA3, histone H2AZ, H2AZ, H2A.F/Z, L000003930, L000004094, YOL012C
Histone variant H2AZ; exchanged for histone H2A in nucleosomes by the SWR1 complex; involved in transcriptional regulation through prevention of the spread of silent heterochromatin; Htz1p-containing nucleosomes facilitate RNA Pol II passage by affecting correct assembly and modification status of RNA Pol II elongation complexes and by favoring efficient nucleosome remodeling
Saccharomyces cerevisiae (S288c)

Biochemical Activity (Acetylation)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

The Saccharomyces cerevisiae histone H2A variant Htz1 is acetylated by NuA4.

Keogh MC, Mennella TA, Sawa C, Berthelet S, Krogan NJ, Wolek A, Podolny V, Carpenter LR, Greenblatt JF, Baetz K, Buratowski S

The histone H2A variant H2A.Z (Saccharomyces cerevisiae Htz1) plays roles in transcription, DNA repair, chromosome stability, and limiting telomeric silencing. The Swr1-Complex (SWR-C) inserts Htz1 into chromatin and shares several subunits with the NuA4 histone acetyltransferase. Furthermore, mutants of these two complexes share several phenotypes, suggesting they may work together. Here we show that NuA4 acetylates Htz1 Lys 14 (K14) ... [more]

Genes Dev. Mar. 15, 2006; 20(6);660-5 [Pubmed: 16543219]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ESA1 HTZ1
Synthetic Growth Defect
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.

Low/High-BioGRID
265512
ESA1 HTZ1
Synthetic Lethality
Synthetic Lethality

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

Low/High-BioGRID
283522

Curated By

  • BioGRID