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TitleStructure of the NuA4 histone acetyltransferase complex.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 119, Issue 48, Page e2214313119, Year 2022
Publish dateNov 29, 2022
AuthorsLiting Ji / Lixia Zhao / Ke Xu / Huihan Gao / Yang Zhou / Roger D Kornberg / Heqiao Zhang /
PubMed AbstractNucleosome acetyltransferase of H4 (NuA4), one of two major histone acetyltransferase complexes in  specifically acetylates histone H2A and H4, resulting in increased transcriptional activity. Here ...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.
External linksProc Natl Acad Sci U S A / PubMed:36417436 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 4.0 Å
Structure data

33794

7yfn

EMDB-33794, PDB-7yfn:
Core module of the NuA4 complex in S. cerevisiae
Method: EM (single particle) / Resolution: 3.8 Å

33796

7yfp

EMDB-33796, PDB-7yfp:
The NuA4 histone acetyltransferase complex from S. cerevisiae
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSFERASE / histone / acetyltransferase / H4 / NuA4 / histone acetyltransferase / acetylation / nucleosome

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