Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Epigenetic mechanisms to propagate histone acetylation by p300/CBP.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 4103, Year 2023
Publish date	Jul 17, 2023
Authors	Masaki Kikuchi / Satoshi Morita / Masatoshi Wakamori / Shin Sato / Tomomi Uchikubo-Kamo / Takehiro Suzuki / Naoshi Dohmae / Mikako Shirouzu / Takashi Umehara /
PubMed Abstract	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 ...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 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 N-terminal tail 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.
External links	Nat Commun / PubMed:37460559 / PubMed Central
Methods	EM (single particle)
Resolution	3.2 - 6.9 Å
Structure data	34588 8hag EMDB-34588, PDB-8hag: Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 1 (3.2 angstrom resolution) Method: EM (single particle) / Resolution: 3.2 Å 34589 8hah EMDB-34589, PDB-8hah: Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 2 (3.9 angstrom resolution) Method: EM (single particle) / Resolution: 3.9 Å EMDB-34590: Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 4 (3.9 angstrom resolution) Method: EM (single particle) / Resolution: 3.9 Å 34591 8hai EMDB-34591, PDB-8hai: Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 1 (4.7 angstrom resolution) Method: EM (single particle) / Resolution: 4.7 Å 34592 8haj EMDB-34592, PDB-8haj: Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 2 (4.8 angstrom resolution) Method: EM (single particle) / Resolution: 4.8 Å EMDB-34593: Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 3 Method: EM (single particle) / Resolution: 6.9 Å 34594 8hak EMDB-34594, PDB-8hak: Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 4 (4.5 angstrom resolution) Method: EM (single particle) / Resolution: 4.5 Å 34595 8hal EMDB-34595, PDB-8hal: Cryo-EM structure of the CBP catalytic core bound to the H4K12acK16ac nucleosome, class 1 Method: EM (single particle) / Resolution: 4.4 Å 34596 8ham EMDB-34596, PDB-8ham: Cryo-EM structure of the CBP catalytic core bound to the H4K12acK16ac nucleosome, class 2 Method: EM (single particle) / Resolution: 4.5 Å 34597 8han EMDB-34597, PDB-8han: Cryo-EM structure of the CBP catalytic core bound to the H4K12acK16ac nucleosome, class 3 Method: EM (single particle) / Resolution: 4.2 Å
Source	homo sapiens (human)
Keywords	TRANSFERASE/DNA / Acetyl taransferase / Complex / Nucleosome / TRANSFERASE / TRANSFERASE-DNA complex