Projects per year
Abstract
Post-translational modifications of proteins have emerged as a major mechanism for regulating gene expression. However, our understanding of how histone modifications directly affect chromatin function remains limited. In this study, we investigate acetylation of histone H3 at lysine 64 (H3K64ac), a previously uncharacterized acetylation on the lateral surface of the histone octamer. We show that H3K64ac regulates nucleosome stability and facilitates nucleosome eviction and hence gene expression in vivo. In line with this, we demonstrate that H3K64ac is enriched in vivo at the transcriptional start sites of active genes and it defines transcriptionally active chromatin. Moreover, we find that the p300 co-activator acetylates H3K64, and consistent with a transcriptional activation function, H3K64ac opposes its repressive counterpart H3K64me3. Our findings reveal an important role for a histone modification within the nucleosome core as a regulator of chromatin function and they demonstrate that lateral surface modifications can define functionally opposing chromatin states. DOI: http://dx.doi.org/10.7554/eLife.01632.001.
Original language | English |
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Article number | e01632 |
Journal | eLife |
Volume | 3 |
DOIs | |
Publication status | Published - 25 Mar 2014 |
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Dive into the research topics of 'Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription'. Together they form a unique fingerprint.Projects
- 2 Finished
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Strategic Award: Wellcome Trust Technology Platform
Blow, J. (Investigator), Lamond, A. (Investigator) & Owen-Hughes, T. (Investigator)
1/01/13 → 30/09/18
Project: Research
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Mechanisms for Remodelling Chromatin (Senior Fellowship Renewal)
Owen-Hughes, T. (Investigator)
1/01/12 → 31/05/19
Project: Research
Profiles
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Owen-Hughes, Tom
- Molecular Cell and Developmental Biology - Professor of Chromatin Structure and Dynamics
Person: Academic