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7YFN

Core module of the NuA4 complex in S. cerevisiae

Summary for 7YFN
Entry DOI10.2210/pdb7yfn/pdb
EMDB information33794
DescriptorActin, ARP4 isoform 1, Chromatin modification-related protein EAF1, ... (7 entities in total)
Functional Keywordshistone, acetyltransferase, h4, nua4, transferase
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Total number of polymer chains6
Total formula weight795335.89
Authors
Ji, L.T.,Zhao, L.X.,Xu, K.,Gao, H.H.,Zhou, Y.,Kornberg, R.D.,Zhang, H.Q. (deposition date: 2022-07-08, release date: 2023-03-08)
Primary citationJi, L.,Zhao, L.,Xu, K.,Gao, H.,Zhou, Y.,Kornberg, R.D.,Zhang, H.
Structure of the NuA4 histone acetyltransferase complex.
Proc.Natl.Acad.Sci.USA, 119:e2214313119-e2214313119, 2022
Cited by
PubMed Abstract: Nucleosome acetyltransferase of H4 (NuA4), one of two major histone acetyltransferase complexes in  specifically acetylates histone H2A and H4, resulting in increased transcriptional activity. Here we present a 3.8-4.0 Å resolution structure of the NuA4 complex from cryoelectron microscopy and associated biochemical studies. The determined structure comprises six subunits and appropriately 5,000 amino acids, with a backbone formed by subunits Eaf1 and Eaf2 spanning from an Actin-Arp4 module to a platform subunit Tra1. Seven subunits are missing from the cryo-EM map. The locations of missing components, Yaf9, and three subunits of the Piccolo module Esa1, Yng2, and Eaf6 were determined. Biochemical studies showed that the Piccolo module and the complete NuA4 exhibit comparable histone acetyltransferase activities, but the Piccolo module binds to nucleosomes, whereas the complete NuA4 does not. The interaction lifetime of NuA4 and nucleosome is evidently short, possibly because of subunits of the NuA4 complex that diminish the affinity of the Piccolo module for the nucleosome, enabling rapid movement from nucleosome to nucleosome.
PubMed: 36417436
DOI: 10.1073/pnas.2214313119
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

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数据于2024-10-30公开中

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