9C4B

Second BAF53a of the human TIP60 complex

9C4B の概要

• エントリーDOI: 10.2210/pdb9c4b/pdb
• EMDBエントリー: 45180
• 分子名称: Actin-like protein 6A (1 entity in total)
• 機能のキーワード: chromatin modification, gene regulation
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47509.81

構造登録者

Yang, Z.,Mameri, A.,Florez Ariza, A.J.,Cote, J.,Nogales, E. (登録日: 2024-06-03, 公開日: 2024-08-14, 最終更新日: 2024-09-11)

主引用文献

Yang, Z.,Mameri, A.,Cattoglio, C.,Lachance, C.,Florez Ariza, A.J.,Luo, J.,Humbert, J.,Sudarshan, D.,Banerjea, A.,Galloy, M.,Fradet-Turcotte, A.,Lambert, J.P.,Ranish, J.A.,Cote, J.,Nogales, E.
Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex.
Science, 385:eadl5816-eadl5816, 2024

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 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.

PubMed: 39088653
DOI: 10.1126/science.adl5816

実験手法

ELECTRON MICROSCOPY (3.4 Å)