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TitleStructural basis for binding diversity of acetyltransferase p300 to the nucleosome.
Journal, issue, pagesiScience, Vol. 25, Issue 7, Page 104563, Year 2022
Publish dateJul 15, 2022
AuthorsSuguru Hatazawa / Jiuyang Liu / Yoshimasa Takizawa / Mohamad Zandian / Lumi Negishi / Tatiana G Kutateladze / Hitoshi Kurumizaka /
PubMed Abstractp300 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.
External linksiScience / PubMed:35754730 / PubMed Central
MethodsEM (single particle)
Resolution3.29 - 3.95 Å
Structure data

32373

7w9v

EMDB-32373, PDB-7w9v:
Cryo-EM structure of nucleosome in complex with p300 acetyltransferase catalytic core (complex I)
Method: EM (single particle) / Resolution: 3.95 Å

EMDB-32374: Cryo-EM structure of nucleosome in complex with p300 acetyltransferase catalytic core (complex II)
Method: EM (single particle) / Resolution: 3.38 Å

EMDB-32375: Cryo-EM structure of nucleosome in complex with p300 acetyltransferase catalytic core (complex III)
Method: EM (single particle) / Resolution: 3.95 Å

EMDB-32376: Cryo-EM structure of nucleosome in complex with p300 acetyltransferase catalytic core (complex IV)
Method: EM (single particle) / Resolution: 3.29 Å

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsGENE REGULATION / p300 / nucleosome / acetyltransferase

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