Structural highlights
Function
H31_HUMAN
Publication Abstract from PubMed
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.
Structural basis for binding diversity of acetyltransferase p300 to the nucleosome.,Hatazawa S, Liu J, Takizawa Y, Zandian M, Negishi L, Kutateladze TG, Kurumizaka H iScience. 2022 Jun 9;25(7):104563. doi: 10.1016/j.isci.2022.104563. eCollection , 2022 Jul 15. PMID:35754730[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hatazawa S, Liu J, Takizawa Y, Zandian M, Negishi L, Kutateladze TG, Kurumizaka H. Structural basis for binding diversity of acetyltransferase p300 to the nucleosome. iScience. 2022 Jun 9;25(7):104563. PMID:35754730 doi:10.1016/j.isci.2022.104563
