+Search query
-Structure paper
Title | Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex. |
---|---|
Journal, issue, pages | Science, Page eadl5816, Year 2024 |
Publish date | Aug 1, 2024 |
![]() | 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 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. |
![]() | ![]() ![]() |
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 |
|
![]() | GENE REGULATION / Chromatin Modification / complex / chromatin regulator |