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-Structure paper
タイトル | Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex. |
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ジャーナル・号・ページ | Science, Page eadl5816, Year 2024 |
掲載日 | 2024年8月1日 |
![]() | 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 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 2.75 - 5.28 Å |
構造データ | EMDB-45176, PDB-9c47: EMDB-45180, PDB-9c4b: EMDB-45206, PDB-9c57: EMDB-45240, PDB-9c62: EMDB-45252, PDB-9c6n: |
化合物 | ![]() ChemComp-AGS: ![]() ChemComp-ATP: ![]() ChemComp-ADP: |
由来 |
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![]() | GENE REGULATION / Chromatin Modification / complex / chromatin regulator |