Proteomics

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Epigenetic mechanisms to propagate histone acetylation by p300/CBP

ABSTRACT: Histone acetylation is important for the activation of gene transcription but little is known about its direct ‘read/write’ mechanisms. Here, we report cryo-electron microscopy structures in which a p300/CBP multidomain monomer recognizes histone H4 N-terminal tail (NT) acetylation (ac) in a nucleosome and acetylates non-H4 histone NTs within the same nucleosome. p300/CBP not only recognized H4NTac via the bromodomain pocket responsible for ‘reading’, but also interacted with the DNA minor grooves via the outside of that pocket. This directed the catalytic center of p300/CBP to one of the non-H4 histone NTs. The primary target that p300 ‘writes’ by ‘reading’ H4NTac was H2BNT, and H2BNTac promoted H2A-H2B dissociation from the nucleosome. We propose a model in which p300/CBP ‘replicates’ histone NT acetylation within the H3-H4 tetramer to inherit epigenetic storage, and ‘transcribes’ it from the H3-H4 tetramer to the H2B-H2A dimers to activate context-dependent gene transcription through local nucleosome destabilization.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Takehiro Suzuki  

LAB HEAD: Naoshi Dohmae

PROVIDER: PXD040835 | Pride | 2023-05-08

REPOSITORIES: Pride

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Hiistone_H2A.mzML Mzml
Hiistone_H2A.mzid.gz Mzid
Hiistone_H2B.mzML Mzml
Hiistone_H2B.mzid.gz Mzid
Hiistone_H3.mzML Mzml
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Epigenetic mechanisms to propagate histone acetylation by p300/CBP.

Kikuchi Masaki M   Morita Satoshi S   Wakamori Masatoshi M   Sato Shin S   Uchikubo-Kamo Tomomi T   Suzuki Takehiro T   Dohmae Naoshi N   Shirouzu Mikako M   Umehara Takashi T  

Nature communications 20230717 1

Histone acetylation is important for the activation of gene transcription but little is known about its direct read/write mechanisms. Here, we report cryogenic electron microscopy structures in which a p300/CREB-binding protein (CBP) multidomain monomer recognizes histone H4 N-terminal tail (NT) acetylation (ac) in a nucleosome and acetylates non-H4 histone NTs within the same nucleosome. p300/CBP not only recognized H4NTac via the bromodomain pocket responsible for reading, but also interacted  ...[more]

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