Structural and Functional Conservation of the NuA4 Histone Acetyltransferase Complex from Yeast to Humans
Open accessAbstract
The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. Its catalytic component, Esa1, is essential for cell cycle progression, gene-specific regulation and has been implicated in DNA repair. Almost all NuA4 subunits have clear homologues in higher eukaryotes, suggesting that the complex is conserved throughout evolution to metazoans. We demonstrate here that NuA4 complexes are indeed present in human cells. Tip60 and its splice variant Tip60b/PLIP were purified as stable HAT complexes associated with identical polypeptides, with 11 of the 12 proteins being homologs of yeast NuA4 subunits. This indicates a highly conserved subunit composition and the identified human proteins underline the role of NuA4 in the control of mammalian cell proliferation. ING3, a member of the ING family of growth regulators, links NuA4 to p53 function which we confirmed in vivo. Proteins specific to the human NuA4 complexes include ruvB-like helicases and a bromodomain-containing subunit linked to ligand-dependent transcription activation by the thyroid hormone receptor. We also demonstrate that subunits MRG15 and DMAP1 are present in distinct protein complexes harboring histone deacetylase and SWI2-related ATPase activities, respectively. Finally, analogous to yeast, a recombinant trimeric complex formed by Tip60, EPC1, and ING3 is sufficient to reconstitute robust nucleosomal HAT activity in vitro. In conclusion, the NuA4 HAT complex is highly conserved in eukaryotes, in which it plays primary roles in transcription, cellular response to DNA damage, and cell cycle control.
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Yeats4 of NuA4 complex is downregulated across all excitatory neurons, indicating repression.
“Conversely, Yeats4 of NuA4 complex is downregulated across all excitatory neurons (Fig. 4f, Supplementary Fig. 6c), indicating repression37.”
From Cell type-specific transcriptional programs in mouse prefrontal cortex during adolescence and addiction (2019) · cites this paper as [37]
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- Authors
- Doyon, Y., Selleck, W., Lane, W. S., Tan, S., & Côté, J.
- Affiliations
- Hôtel-Dieu de Québec (CA)
- Pennsylvania State University (US)
- Harvard University (US)
- Corresponding author
- Côté, Jacques
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2004-03-01
- Volume
- 24
- Issue
- 5
- Pages
- 1884-1896
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC350560
- OpenAlex
- W2111578933
- Cited by
- 597
- References
- 65
- Citations by year
- 2026: 18 · 2025: 25 · 2024: 25 · 2023: 34 · 2022: 24 · 2021: 28 · 2020: 31 · 2019: 21 · 2018: 24 · 2017: 33 · 2016: 13 · 2015: 21 · 2014: 26 · 2013: 21 · 2012: 26
- FWCI
- 13.05
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Génome Québec
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- Tip60, Esa1, evolutionary conservation, histone H4 acetylation, ING3, p53, bromodomain, thyroid hormone receptor, MRG15, histone deacetylase, cell cycle regulation, DNA damage response, transcriptional regulation
- MeSH terms
- Lysine Acetyltransferase 5, Acetylation, Acetyltransferases, Amino Acid Sequence, Animals, Carrier Proteins, Cell Cycle, Cell Line, DNA Helicases, Histones, Humans, Molecular Sequence Data, Multienzyme Complexes, Proteins, Repressor Proteins, Transcription Factors, Trans-Activators, Genes, Tumor Suppressor, Sequence Alignment, Homeodomain Proteins, Protein Subunits, Tumor Suppressor Proteins, Saccharomyces cerevisiae Proteins, Histone Acetyltransferases
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