Selective Requirements for Histone H3 and H4 N Termini in p300-Dependent Transcriptional Activation from Chromatin
Open accessAbstract
The N-terminal tails of the core histones play important roles in transcriptional regulation, but their mechanism(s) of action are poorly understood. Here, pure chromatin templates assembled with varied combinations of recombinant wild-type and mutant core histones have been employed to ascertain the role of individual histone tails, both in overall acetylation patterns and in transcription. In vitro assays show an indispensable role for H3 and H4 tails, especially major lysine substrates, in p300-dependent transcriptional activation, as well as activator-targeted acetylation of promoter-proximal histone tails by p300. These results indicate, first, that constraints to transcription are imposed by nucleosomal histone components other than histone N-terminal tails and, second, that the histone N-terminal tails have selective roles, which can be modulated by targeted acetylation, in transcriptional activation by p300.
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JQ1 treatment causes a time-dependent decrease in the activating H3K27ac mark, consistent with the trend of transcriptional downregulation.
“Interestingly, JQ1 treatment elicited a time-dependent decrease in the activating H3K27ac mark19, consistent with the observed trend in transcriptional downregulation (Fig. 3F and Supplementary Fig. 13A–E).”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [19]
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- Authors
- An, W., Palhan, V. B., Karymov, M. A., Leuba, S. H., & Roeder, R. G.
- Affiliations
- Rockefeller University (US)
- National Institutes of Health (US)
- Corresponding author
- Roeder, Robert G
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2002-04
- Volume
- 9
- Issue
- 4
- Pages
- 811-821
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2047534579
- Cited by
- 100
- References
- 65
- Citations by year
- 2024: 1 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 6 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 2 · 2014: 1 · 2013: 3
- FWCI
- 5.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- 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 › Epigenetics and DNA Methylation
- Keywords
- histone H3 N-terminal tail, P300, transcriptional activation, histone acetylation, chromatin templates, nucleosome
- MeSH terms
- Acetylation, Amino Acid Sequence, Animals, Chromatin, Histones, Models, Genetic, Molecular Sequence Data, Nuclear Proteins, Nucleosomes, Precipitin Tests, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Structure-Activity Relationship, Templates, Genetic, Xenopus laevis, Transcriptional Activation, Trans-Activators, Protein Structure, Tertiary
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