Specific Contributions of Histone Tails and their Acetylation to the Mechanical Stability of Nucleosomes
Abstract
The distinct contributions of histone tails and their acetylation to nucleosomal stability were examined by mechanical disruption of individual nucleosomes in a single chromatin fiber using an optical trap. Enzymatic removal of H2A/H2B tails primarily decreased the strength of histone-DNA interactions located approximately +/-36bp from the dyad axis of symmetry (off-dyad strong interactions), whereas removal of the H3/H4 tails played a greater role in regulating the total amount of DNA bound. Similarly, nucleosomes composed of histones acetylated to different degrees by the histone acetyltransferase p300 exhibited significant decreases in the off-dyad strong interactions and the total amount of DNA bound. Acetylation of H2A/H2B appears to play a particularly critical role in weakening the off-dyad strong interactions. Collectively, our results suggest that the destabilizing effects of tail acetylation may be due to elimination of specific key interactions in the nucleosome.
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The relationship between TF occupancy and gene expression can be well fit by modifying the telegraph model to include a promoter on-rate proportional to the average number of TFs bound (Additive Activation model).
“This relationship between TF occupancy and gene expression can be well fit by modifying the commonly-used “telegraph” model of transcription31–33, which assumes that promoters can be either “on” (transcribing) or “off”, to include a promoter on-rate that is proportional to the average number of TFs bound (Additive Activation model; Fig. 3F, Methods)”
From Single-molecule states link transcription factor binding to gene expression (2024) · cites this paper as [31]
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Single-molecule states link transcription factor binding to gene expression
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- Authors
- Brower-Toland, B., Wacker, D. A., Fulbright, R. M., Lis, J. T., Kraus, W. L., & Wang, M. D.
- Affiliations
- Cornell University (US)
- Corresponding author
- Wang, Michelle D.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2005-02
- Volume
- 346
- Issue
- 1
- Pages
- 135-146
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2146716725
- Cited by
- 198
- References
- 2
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 10 · 2023: 5 · 2022: 5 · 2021: 7 · 2020: 8 · 2019: 10 · 2018: 7 · 2017: 5 · 2016: 17 · 2015: 8 · 2014: 10 · 2013: 9 · 2012: 10
- FWCI
- 4.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Cancer Society
- W. M. Keck Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (GM-25232)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- nucleosome stability, histone tails, histone acetylation, histone-DNA interactions, P300, histone acetyltransferase, optical tweezers, DNA binding
- MeSH terms
- Acetylation, Amino Acid Sequence, DNA, Gene Expression Regulation, Histones, Humans, Molecular Sequence Data, Nucleosomes, Thermodynamics, Transcription, Genetic, Microarray Analysis
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