Proteomics

Dataset Information

0

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

Json Xml
altmetric image

Publications

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]

Similar Datasets

Unknown Acetylation of histone H2B marks active enhancers and predicts CBP/p300 target genes
2023-02-23 | GSE186349 | GEO
Proteomics Molecular basis of RanGTP-activated release of Histones H2A-H2B from Importin-9
2023-06-02 | PXD037571 | Pride
Proteomics Nut interactome in round/elongating spermatids
2018-10-02 | PXD008727 | Pride
Unknown Recycling of H2A-H2B provides short-term memory of chromatin states [SCAR-Seq]
2023-02-06 | GSE204984 | GEO
Unknown Recycling of H2A-H2B provides short-term memory of chromatin states [ChOR-Seq]
2023-02-06 | GSE204981 | GEO
Unknown Recycling of H2A-H2B provides short-term memory of chromatin states [ChIP-Seq]
2023-02-06 | GSE204974 | GEO
Proteomics Nuclear condensates of p300 formed though the structured catalytic core can act as a storage pool of p300 with reduced HAT activity
2021-08-26 | PXD026898 | Pride
Genomics High-throughput sequence data of ChIP performed with anti-SMARCAD1 (ASNA) or anti-CBP actibodies.
2016-03-17 | E-GEOD-72666 | biostudies-arrayexpress
Proteomics Time-resolved analysis reveals rapid dynamics and broad scope of the CBP/p300 acetylome
2018-06-10 | PXD005252 | Pride
Transcriptomics Transcription profiling of human embryonic kidney cells overexpressing SMYD2 to identify which genes are regulated by SMYD2 through its histone lysine methylation activity
2008-02-05 | E-MEXP-963 | biostudies-arrayexpress