9C47

TRRAP module of the human TIP60 complex

Summary for 9C47

• Entry DOI: 10.2210/pdb9c47/pdb
• EMDB information: 45176
• Descriptor: Transformation/transcription domain-associated protein, E1A-binding protein p400 (2 entities in total)
• Functional Keywords: chromatin modification, gene regulation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 782006.84

Authors

Yang, Z.,Mameri, A.,Florez Ariza, A.J.,Cote, J.,Nogales, E. (deposition date: 2024-06-03, release date: 2024-08-14, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.4 Å)