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Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [RNA-seq]

GSE261651 Homo sapiens Expression profiling by high throughput sequencing 6 samples Submitted 2024/08/06 Platform GPL18573
Summary
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 play crucial roles regulating gene expression and maintaining genome stability. Our cryo-EM studies show that within the NuA4/TIP60 complex, the EP400 subunit serves as an architectural scaffold holding the different functional modules in specific positions and giving rise to a novel arrangement of the ARP module. EP400 interacts with the TRRAP subunit using a footprint that overlaps with that of the SAGA acetyltransferase complex, thereby 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.
Published in
Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex
Yang Z, Mameri A, Cattoglio C et al. · Science (New York, N.Y.) 2024 · PMID 39088653 · doi:10.1126/science.adl5816
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Also filed as BioProject PRJNA1088181 and SRA study SRP495342. Searching any of these in the dataset finder brings you back here.

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