Literature summary for 2.3.1.48 extracted from

Dacquay, L.; Flint, A.; Butcher, J.; Salem, D.; Kennedy, M.; Kaern, M.; Stintzi, A.; Baetz, K.
NuA4 lysine acetyltransferase complex contributes to phospholipid homeostasis in Saccharomyces cerevisiae (2017), G3 (Bethesda), 7, 1799-1809 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
lipid droplet	-	Saccharomyces cerevisiae	5811	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Saccharomyces cerevisiae	NuA4 targets histone and nonhistone proteins	?	-	-
additional information	Saccharomyces cerevisiae BY4741	NuA4 targets histone and nonhistone proteins	?	-	-

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q08649	NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1	-
Saccharomyces cerevisiae BY4741	Q08649	NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	NuA4 targets histone and nonhistone proteins	Saccharomyces cerevisiae	?	-	-
additional information	NuA4 targets histone and nonhistone proteins	Saccharomyces cerevisiae BY4741	?	-	-

Subunits

Subunits	Comment	Organism
multimer	the NuA4 histone acetyltransferase complex is composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2 subunits	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
lysine acetyltransferase complex	-	Saccharomyces cerevisiae
NuA4	the NuA4 histone acetyltransferase complex is composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2 subunits	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
acetyl-CoA	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
malfunction	NuA4 mutants induce the expression of the inositol-3-phosphate synthase gene, INO1, which leads to excessive accumulation of inositol, a key metabolite used for phospholipid biosynthesis, called an Opi- phenotype. High-throughput genomic screens have identified many other mutants that derepress INO1 transcription, besides Opil mutants, and cause excessive accumulation of inositol, including mutants of the NuA4 complex (EAF1, EAF3, EAF5, EAF7, YAF9, and ESA1). NuA4 mutants exacerbate the growth defects of sec14-1ts under inositol-depleted conditions. As NuA4 mutants exhibit a derepression of INO1 and excessive inositol production, or Opi- phenotype, NuA4 mutants suppress the growth defect in sec14-1ts under inositol-depleted conditions. Lipid droplet dynamics are impaired in eaf1DELTA cells. The eaf1DELTA mutant negative genetic interaction with sec14-1ts and the decreased lipid droplet staining in eaf1D originate from defects within the fatty acid biosynthesis pathway	Saccharomyces cerevisiae
metabolism	analysis of connections between NuA4, inositol, and Sec14, which is a phosphatidylinositol/phosphatidylcholine transfer protein. Overview of phospholipid metabolism. Sec14 (UniProt ID P24280) is an essential phospholipid-binding protein that coordinates the metabolism of phosphatidylinositol-4-phosphate with phosphatidylcholine (PC) at the Golgi to create a lipid environment necessary for trafficking events	Saccharomyces cerevisiae
additional information	NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1 and held together by the scaffolding protein Eaf1	Saccharomyces cerevisiae
physiological function	the lysine acetyltransferase complex NuA4 plays a role in phospholipid homeostasis. One role for NuA4 is the regulation of chromatin remodeling and gene transcription through the acetylation of histones H4 andH2A-Z, and NuA4 also targets nonhistone proteins	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)