HdaA, a Major Class 2 Histone Deacetylase of Aspergillus nidulans , Affects Growth under Conditions of Oxidative Stress
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Histone deacetylases (HDACs) catalyze the removal of acetyl groups from the ε-amino group of distinct lysine residues in the amino-terminal tail of core histones. Since the acetylation status of core histones plays a crucial role in fundamental processes in eukaryotic organisms, such as replication and regulation of transcription, recent research has focused on the enzymes responsible for the acetylation/deacetylation of core histones. Very recently, we showed that HdaA, a member of the Saccharomyces cerevisiae HDA1-type histone deacetylases, is a substantial contributor to total HDAC activity in the filamentous fungus Aspergillus nidulans. Now we demonstrate that deletion of the hdaA gene indeed results in the loss of the main activity peak and in a dramatic reduction of total HDAC activity. In contrast to its orthologs in yeast and higher eukaryotes, HdaA has strong intrinsic activity as a protein monomer when expressed as a recombinant protein in a prokaryotic expression system. In vivo, HdaA is involved in the regulation of enzymes which are of vital importance for the cellular antioxidant response in A. nidulans . Consequently, Δ hdaA strains exhibit significantly reduced growth on substrates whose catabolism generates molecules responsible for oxidative stress conditions in the fungus. Our analysis revealed that reduced expression of the fungal catalase CatB is jointly responsible for the significant growth reduction of the hdaA mutant strains.
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Deletion of hdaA led to a major defect of KDAC activity and hypersensitivity to oxidative stress in A. nidulans.
“Deletion of hdaA led to a major defect of KDAC activity and hypersensitivity to oxidative stress (39).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [39]
Analyses of the KDAC activity pattern in fungi revealed important differences among yeasts and molds.
“Analyses of the KDAC activity pattern in fungi revealed important differences among yeasts and molds (39, 40), which could explain these discrepancies.”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [39]
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- Authors
- Tribus, M., Galehr, J., Trojer, P., Brosch, G., Loidl, P., Marx, F., Haas, H., & Graessle, S.
- Affiliations
- Innsbruck Medical University (AT)
- Corresponding author
- Graessle, Stefan
- Venue
- Eukaryotic Cell
- Publisher
- American Society for Microbiology
- Published
- 2005-10
- Volume
- 4
- Issue
- 10
- Pages
- 1736-1745
- ISSN
- 1535-9778 (ISSN-L)
- 1535-9786
- PMC
- PMC1265891
- OpenAlex
- W2140680341
- Cited by
- 67
- References
- 63
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 3 · 2023: 2 · 2022: 8 · 2021: 5 · 2020: 6 · 2019: 5 · 2018: 5 · 2017: 2 · 2016: 3 · 2015: 4 · 2014: 4 · 2013: 2 · 2012: 1
- FWCI
- 0.50
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Eukaryotic Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Oesterreichische Nationalbank
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- histone deacetylase, Aspergillus nidulans, oxidative stress, antioxidant response, fungal growth, recombinant protein expression
- MeSH terms
- Aspergillus nidulans, Catalase, Fungal Proteins, Histone Deacetylases, Hydrogen Peroxide, Mutation, Phenotype, Oxidants, Reactive Oxygen Species, Oxidative Stress, Hyphae
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