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Cloning and Characterization of a Novel Human Class I Histone Deacetylase That Functions as a Transcription Repressor
Open accessAbstract
Histone acetylation alters chromatin state by modifying lysines on histone and plays an important role in modulating gene transcription. A dynamic balance of histone acetylation/deacetylation is maintained by histone acetyltransferases and histone deacetylases. Emerging evidence suggests that a family of histone deacetylases may exist to regulate diverse cellular functions, including chromatin structure, gene expression, cell cycle progression, and oncogenesis. We describe here a novel human histone deacetylase, named HDAC8, cloned from human kidney. HDAC8 encodes 377 amino acid residues and shares extensive homology to several known HDACs, in particular a histone deacetylase from Arabidopsis thaliana. Northern blot analyses revealed that HDAC8 expression pattern for HDAC8 is distinct from that for HDAC1 and HDAC3, and expression of HDAC8 mRNA occurs in multiple organs including heart, lung, kidney, and pancreas. HDAC8 mRNA was also observed in several cell lines derived from cancerous tissues. When expressed in HEK293 cells, HDAC8 exhibited deacetylase activity toward acetylated histone, indicating that this protein is a bona fide histone deacetylase. Its histone deacetylase activity was inhibited by trichostatin and other known histone deacetylase inhibitors. Furthermore, active recombinant HDAC8 was expressed and purified from Escherichia coli. When ectopically expressed in cells, HDAC8 was found to be localized to the nucleus. Co-transfection experiments demonstrated that expression of HDAC8 repressed a viral SV40 early promoter activity. These results indicate that HDAC8 is a novel member of the histone deacetylase family, which may play a role in the development of a broad range of tissues and potentially in the etiology of cancer.
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“Of these, only HDAC8 is a fully functional enzyme in isolation5,6.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [5]
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“The finding of a direct involvement of K+ ions in the architecture of the active site and in the stabilization of structural elements of HDAC8 could rationalize previously observed potassium dependence of the activity of this enzyme ([12](#ref12)) and of other subtypes (P.G., unpublished results).”
From Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor (2004) · cites this paper as [12]
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Self-citation
Metadata
- Authors
- Hu, E., Chen, Z., Fredrickson, T., Zhu, Y., Kirkpatrick, R., Zhang, G.-F., Johanson, K., Sung, C.-M., Liu, R., & Winkler, J.
- Corresponding author
- Hu, Erding
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-05
- Volume
- 275
- Issue
- 20
- Pages
- 15254-15264
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2061360494
- Cited by
- 309
- References
- 80
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 11 · 2023: 22 · 2022: 12 · 2021: 8 · 2020: 18 · 2019: 8 · 2018: 9 · 2017: 10 · 2016: 10 · 2015: 14 · 2014: 12 · 2013: 11 · 2012: 14
- FWCI
- 6.87
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- HDAC8, histone deacetylase, class I histone deacetylases, transcriptional repression, histone acetylation, chromatin regulation, gene expression regulation, histone deacetylase inhibitors, SV40 early promoter, nuclear localization, tissue-specific gene expression, cancer
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, Histone Deacetylases, Humans, Kidney, Molecular Sequence Data, Organ Specificity, Phylogeny, Recombinant Proteins, Repressor Proteins, RNA, Messenger, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Sequence Alignment, 3T3 Cells, Arabidopsis, Sequence Homology, Amino Acid, Mice
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