The BAF complex enhances transcription through interaction with H3K56ac in the histone globular domain

Kwangbeom Hyun, Jihye Ahn, Hyoungmin Kim, Jihyun Kim, Yong-In Kim, Hee-Sung Park, Robert G. Roeder, J. Eugene Lee () and Jaehoon Kim ()
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Kwangbeom Hyun: Korea Advanced Institute of Science and Technology
Jihye Ahn: Korea Advanced Institute of Science and Technology
Hyoungmin Kim: Korea Advanced Institute of Science and Technology
Jihyun Kim: Korea Advanced Institute of Science and Technology
Yong-In Kim: Korea Research Institute of Standards and Science
Hee-Sung Park: Korea Advanced Institute of Science and Technology
Robert G. Roeder: The Rockefeller University
J. Eugene Lee: Korea Research Institute of Standards and Science
Jaehoon Kim: Korea Advanced Institute of Science and Technology

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Histone post-translational modifications play pivotal roles in eukaryotic gene expression. To date, most studies have focused on modifications in unstructured histone N-terminal tail domains and their binding proteins. However, transcriptional regulation by chromatin-effector proteins that directly recognize modifications in histone globular domains has yet to be clearly demonstrated, despite the richness of their multiple modifications. Here, we show that the ATP-dependent chromatin-remodeling BAF complex stimulates p53-dependent transcription through direct interaction with H3K56ac located on the lateral surface of the histone globular domain. Mechanistically, the BAF complex recognizes nucleosomal H3K56ac via the DPF domain in the DPF2 subunit and exhibits enhanced nucleosome-remodeling activity in the presence of H3K56ac. We further demonstrate that a defect in H3K56ac–BAF complex interaction leads to impaired p53-dependent gene expression and DNA damage responses. Our study provides direct evidence that histone globular domain modifications participate in the regulation of gene expression.

Date: 2024
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DOI: 10.1038/s41467-024-53981-0

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