Cited by 1,732Genomics and Chromatin DynamicsProtein Degradation and InhibitorsProtein Structure and Dynamics

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Structure and ligand of a histone acetyltransferase bromodomain

Dhalluin, Christophe, Carlson, Justin E., Zeng, Lei, He, Cheng, Aggarwal, Aneel K., Zhou, Ming-Ming, Zhou, Ming-Ming·1999·Nature

DOI 10.1038/20974

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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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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)
ORCID: Zeng, Lei
Aggarwal, Aneel K.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1999-06
Volume: 399
Issue: 6735
Pages: 491-496
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/20974
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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Structure and ligand of a histone acetyltransferase bromodomain

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