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Crosslinking mass spectrometry of the p300 catalytic core complexed with the nucleosome

ABSTRACT: p300 is a histone acetyltransferase that associates with crucial biological processes. p300 acetylates all four histones in the nucleosome, a basic unit of chromatin, and alters chromatin structure and dynamics. In this study, we performed structural and biochemical analysis to understand the nucleosome binding by p300. Crosslinking mass spectrometry suggests that the p300 catalytic core binds to nucleosomes in multiple binding forms to acetylate different histone tails.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hitoshi Kurumizaka

PROVIDER: PXD033804 | JPOST Repository | Wed Jun 29 00:00:00 BST 2022

REPOSITORIES: jPOST

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Structural basis for binding diversity of acetyltransferase p300 to the nucleosome.

Hatazawa Suguru S Liu Jiuyang J Takizawa Yoshimasa Y Zandian Mohamad M Negishi Lumi L Kutateladze Tatiana G TG Kurumizaka Hitoshi H

iScience 20220609 7

p300 is a human acetyltransferase that associates with chromatin and mediates vital cellular processes. We now report the cryo-electron microscopy structures of the p300 catalytic core in complex with the nucleosome core particle (NCP). In the most resolved structure, the HAT domain and bromodomain of p300 contact nucleosomal DNA at superhelical locations 2 and 3, and the catalytic site of the HAT domain are positioned near the N-terminal tail of histone H4. Mutations of the p300-DNA interfacial ...[more]

PMID: 35754730

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