The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Structure and ligand of a histone acetyltransferase bromodomain
Abstract
Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.
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“However, Lys-ac and Lys-cr may be interpreted differently, since they are recognized by distinct readers, in the bromodomain10 and Yeats domain11 respectively.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [10]
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The role of enhancer RNAs in epigenetic regulation of gene expression
Rahnamoun, H., Orozco, P., & Lauberth, S. M. (2020) · Transcription · doi:10.1080/21541264.2019.1698934 · Cited by 16
Metadata
- Authors
- Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., Zhou, M.-M., & Zhou, M.-M.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Venue
- Nature
- Published
- 1999-06
- Volume
- 399
- Issue
- 6735
- Pages
- 491-496
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1625510017
- Cited by
- 1,732
- References
- 30
- Citations by year
- 2026: 50 · 2025: 58 · 2024: 68 · 2023: 75 · 2022: 64 · 2021: 74 · 2020: 75 · 2019: 80 · 2018: 85 · 2017: 84 · 2016: 100 · 2015: 66 · 2014: 67 · 2013: 63 · 2012: 50
- FWCI
- 25.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- bromodomain, histone acetyltransferase, PCAF, protein structure, four-helix bundle, histone acetylation, transcriptional regulation, acetyl-CoA binding
- MeSH terms
- p300-CBP-Associated Factor, Acetyltransferases, Amino Acid Sequence, Escherichia coli, Ligands, Lysine, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Recombinant Proteins, Transcription Factors, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Bromine Compounds, Crystallography, X-Ray, Cell Cycle Proteins, Saccharomyces cerevisiae Proteins, p300-CBP Transcription Factors, Histone Acetyltransferases
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