Japan Agency for Medical Research and Development (AMED)
JP21am0101076
Japan
Japan Agency for Medical Research and Development (AMED)
JP20am0101115j0004
Japan
Japan Science and Technology
JPMJER1901
Japan
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM135671
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM125195
United States
National Institutes of Health/National Cancer Institute (NIH/NCI)
CA252707
United States
National Institutes of Health/National Institute on Aging (NIH/NIA)
AG067664
United States
Japan Agency for Medical Research and Development (AMED)
JP22ama121009
Japan
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
HL151334
United States
Citation
Journal: iScience / Year: 2022 Title: Structural basis for binding diversity of acetyltransferase p300 to the nucleosome. Authors: Suguru Hatazawa / Jiuyang Liu / Yoshimasa Takizawa / Mohamad Zandian / Lumi Negishi / Tatiana G Kutateladze / Hitoshi Kurumizaka / Abstract: 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 ...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 residues of p300 substantially decrease binding to NCP. Three additional classes of p300-NCP complexes show different modes of the p300-NCP complex formation. Our data provide structural details critical to our understanding of the mechanism by which p300 acetylates multiple sites on the nucleosome.
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