Histone deacetylase 1 activates PU.1 gene transcription through regulating TAF9 deacetylation and transcription factor IID assembly
Open accessAbstract
Histone acetyltransferases and histone deacetylases (HDACs) are important epigenetic coregulators. It has been thought that HDACs associate with corepressor complexes and repress gene transcription; however, in this study, we have found that PU.1—a key master regulator for hematopoietic self‐renewal and lineage specification—requires HDAC activity for gene activation. Deregulated PU.1 gene expression is linked to dysregulated hematopoiesis and the development of leukemia. In this study, we used erythroid differentiation as a model to analyze how the PU.1 gene is regulated. We found that active HDAC1 is directly recruited to active PU.1 promoter in progenitor cells, whereas acetylated HDAC1, which is inactive, is on the silenced PU.1 promoter in differentiated erythroid cells. We then studied the mechanism of HDAC1‐mediated activation. We discovered that HDAC1 activates PU.1 gene transcription via deacetylation of TATA‐binding protein–associated factor 9 (TAF9), a component in the transcription factor IID (TFIID) complex. Treatment with HDAC inhibitor results in an increase in TAF9 acetylation. Acetylated TAF9 does not bind to the PU.1 gene promoter and subsequently leads to the disassociation of the TFIID complex and transcription repression. Thus, these results demonstrate a key role for HDAC1 in PU.1 gene transcription and, more importantly, uncover a novel mechanism of TFIID recruitment and gene activation.—Jian, W., Yan, B., Huang, S., Qiu, Y. Histone deacetylase 1 activates PU.1 gene transcription through regulating TAF9 deacetylation and transcription factor IID assembly. FASEB J. 31, 4104–4116 (2017). www.fasebj.org —Jian, Wei, Yan, Bowen, Huang, Suming, Qiu, Yi Histone deacetylase 1 activates PU.1 gene transcription through regulating TAF9 deacetylation and transcription factor IID assembly. FASEB J. 31, 4104–4116 (2017)
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Chen, J., Dong, B., Xie, Y., et al. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06809-4 · Cited by 1 · see citing works
Targeting Epigenetic Modifiers for Cancer Treatments
Chee, C. S., & Leung, D. (2018) · Current Pharmacology Reports · doi:10.1007/s40495-018-0130-9 · Cited by 1 · see citing works
Takao, S., Forbes, L., Uni, M., Cheng, S., Pineda, J. M. B., Tarumoto, Y., Cifani, P., Minuesa, G., Chen, C., Kharas, M. G., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.05.077156
- Authors
- Jian, W., Yan, B., Huang, S., & Qiu, Y.
- Affiliations
- University of Florida Health (US)
- Macau University of Science and Technology (MO)
- Corresponding author
- Qiu, Yi
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2017-09
- Volume
- 31
- Issue
- 9
- Pages
- 4104-4116
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- PMC
- PMC5572695
- OpenAlex
- W2621247544
- Semantic Scholar
- 69adf2983cd22decc0ea71b423ce543b94ec936d
- Cited by
- 23
- References
- 70
- Citations by year
- 2025: 2 · 2024: 2 · 2022: 2 · 2021: 4 · 2020: 5 · 2019: 4 · 2018: 3 · 2017: 1
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (submittedVersion)
- PubMed Central (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01-HL095674)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01-DK110108)
- American Heart Association (AHA16GRNT31020032)
- Bankhead-Coley Foundation
- 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
- HDAC1, PU.1, transcription factor IID, transcriptional activation, histone deacetylation, erythroid differentiation, hematopoiesis, leukemia
- MeSH terms
- RAW 264.7 Cells, Proto-Oncogene Protein Spi-1, Animals, Erythropoiesis, Humans, Protein Binding, Proto-Oncogene Proteins, T-Lymphocytes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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