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ProteomicsUnique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex
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...
ORGANISM(S): Homo sapiens (Human) 
2024-08-08 | PXD053209 | Pride
Nua4/tip60 acetyltransferase P400-ncp complex H2a.z Nua4 and swr1 chromatin modifier and remodeler complexes 
ProteomicsAn NPAS4:NuA4 complex couples synaptic activity to DNA repair
Neuronal activity is critical for adaptive circuit remodeling but poses an inherent risk to the stability of the genome across the long lifespan of post-mitotic neurons1-5. Whether neurons have acquired specialized genome protection mechanisms that enable them to withstand decades of potentially dam...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-02-15 | PXD038718 | Pride
Nua4 Mus musculus Hippocampus Tip60 Hek293t Npas4 
ProteomicsUnique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex
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...
ORGANISM(S): Homo sapiens (Human) 
2024-08-08 | PXD053207 | Pride
Nua4/tip60 acetyltransferase Ep400 complex Chromatin remodeling complex Ncp 
ProteomicsNuA4 and SWR1 complex in Plasmodium falciparum
In this study, we identified an MYST-associated complex in P. falciparum, which contains 11 of 13 conserved NuA4 subunits based on their domain structures. Meanwhile, reciprocal pulldowns not only confirmed the NuA4-like complex but also identified an SWR1-like complex, a histone remodeling complex,...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2024-03-18 | PXD046547 | Pride
Plasmodium Nua4 Dna repair Swr1 
ProteomicsDrosophila SWR1 and NuA4 complexes are defined by DOMINO isoform
Histone acetylation and deposition of H2A.Z variant are integral aspects of active transcrip-tion. In Drosophila, the single DOMINO chromatin regulator complex is thought to combine both activities via an unknown mechanism. Here we show that alternative isoforms of the DOMINO nucleosome remodeling A...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2020-05-27 | PXD017729 | Pride
Nua4 Drosophila Domino H3ac Swr1 H4ac 
UnknownStructure and nucleosome interaction of the yeast NuA4 and Piccolo-NuA4 histone acetyltransferase complexes.
Not available
S-EPMC3210417 | biostudies-literature
ProteomicsNuA4 and H2A.Z control environmental responses and autotrophic growth in Arabidopsis
Nucleosomal acetyltransferase of H4 (NuA4) is an essential transcriptional coactivator in eukaryotes, but remains poorly characterized in plants. Here, we describe Arabidopsis homologs of the NuA4 scaffold proteins Enhancer of Polycomb-Like-1 (AtEPL1) and Esa1- Associated Factor 1 (AtEAF1). Loss of ...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2021-12-20 | PXD030302 | Pride
Nua4 / eaf1 / epl1 / h4 acetylation / h2a.z acetylation / h2a.z deposition / photosynthesis / stress response 
TranscriptomicsEaf7 identifies a native protein trimer linked to RNA polymerase-coupled nucleosome recycling
The NuA4 histone acetyltransferase (HAT) complex is required for gene specific regulation, cell cycle progression, and DNA repair. Dissection of the 13-subunit complex reveals that the Eaf7 subunit bridges Eaf5 with Eaf3, a H3K36me3-binding chromodomain protein, and this Eaf5/7/3 trimer is anchored ...
ORGANISM(S): Saccharomyces cerevisiae 
2014-09-25 | E-MTAB-1780 | biostudies-arrayexpress
GenomicsNuA4 and H2A.Z control environmental responses and autotrophic growth in Arabidopsis
NuA4 and H2A.Z control environmental responses and autotrophic growth in Arabidopsis
PRJNA641025 | ENA
UnknownStructure of the NuA4 histone acetyltransferase complex.
Not available
S-EPMC9860254 | biostudies-literature
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