+Search query
-Structure paper
Title | Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex. |
---|---|
Journal, issue, pages | Science, Vol. 385, Issue 6711, Page eadl5816, Year 2024 |
Publish date | Aug 23, 2024 |
Authors | Zhenlin 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 Abstract | The human nucleosome acetyltransferase of histone H4 (NuA4)/Tat-interactive protein, 60 kilodalton (TIP60) coactivator complex, a fusion of the yeast switch/sucrose nonfermentable related 1 (SWR1) ...The human nucleosome acetyltransferase of histone H4 (NuA4)/Tat-interactive protein, 60 kilodalton (TIP60) coactivator complex, a fusion of the yeast switch/sucrose nonfermentable related 1 (SWR1) and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4, H2A, and H2A.Z to regulate gene expression and maintain genome stability. Our cryo-electron microscopy studies show that, within the NuA4/TIP60 complex, the E1A binding protein P400 (EP400) subunit serves as a scaffold holding the different functional modules in specific positions, creating a distinct arrangement of the actin-related protein (ARP) module. EP400 interacts with the transformation/transcription domain-associated protein (TRRAP) subunit by using a footprint that overlaps with that of the Spt-Ada-Gcn5 acetyltransferase (SAGA) 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 links | Science / PubMed:39088653 |
Methods | EM (single particle) |
Resolution | 2.75 - 5.28 Å |
Structure data | EMDB-45176, PDB-9c47: EMDB-45180, PDB-9c4b: EMDB-45206, PDB-9c57: EMDB-45240, PDB-9c62: EMDB-45252, PDB-9c6n: |
Chemicals | ChemComp-AGS: ChemComp-ATP: ChemComp-ADP: |
Source |
|
Keywords | GENE REGULATION / Chromatin Modification / complex / chromatin regulator |