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TitleStructural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex.
Journal, issue, pagesScience, Page eadl5816, Year 2024
Publish dateAug 1, 2024
AuthorsZhenlin Yang / Amel Mameri / Claudia Cattoglio / Catherine Lachance / Alfredo Jose Florez Ariza / Jie Luo / Jonathan Humbert / Deepthi Sudarshan / Arul Banerjea / Maxime Galloy / Amélie Fradet-Turcotte / Jean-Philippe Lambert / Jeff A Ranish / Jacques Côté / Eva Nogales /
PubMed AbstractThe human NuA4/TIP60 co-activator complex, a fusion of the yeast SWR1 and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4/H2A/H2A.Z to regulate ...The human NuA4/TIP60 co-activator complex, a fusion of the yeast SWR1 and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4/H2A/H2A.Z to regulate gene expression and maintain genome stability. Our cryo-electron microscopy studies show that, within the NuA4/TIP60 complex, the EP400 subunit serves as a scaffold holding the different functional modules in specific positions, creating a unique arrangement of the ARP module. EP400 interacts with the TRRAP subunit using a footprint that overlaps with that of the SAGA acetyltransferase complex, preventing the formation of a hybrid complex. Loss of the TRRAP subunit leads to mislocalization of NuA4/TIP60, resulting in the redistribution of H2A.Z and its acetylation across the genome, emphasizing the dual functionality of NuA4/TIP60 as a single macromolecular assembly.
External linksScience / PubMed:39088653
MethodsEM (single particle)
Resolution3.4 Å
Structure data

45176
EMDB entry, No image

9c47

EMDB-45176, PDB-9c47:
TRRAP module of the human TIP60 complex
Method: EM (single particle) / Resolution: 3.4 Å

45180
EMDB entry, No image

9c4b

EMDB-45180, PDB-9c4b:
Second BAF53a of the human TIP60 complex
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • homo sapiens (human)
KeywordsGENE REGULATION / Chromatin Modification

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