Proteomics

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Yang_NuA4_TIP60_structural_features

ABSTRACT: This submission contains the mass spectrometry files for the manuscript by Zhenlin Yang et al. that describes the unique structural features of the NuA4/TIP60 acetyltransferase and chromatin remodeling complex. MS experiments were performed from TAP purified complexes from K562 cells and MS files were acquired on Orbitrap Fusion mass spectrometers. For questions, please contact Jean-Philippe Lambert (Jean-Philippe.Lambert@crchudequebec.ulaval.ca).

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Jean-Philippe Lambert  

PROVIDER: MSV000093280 | MassIVE | Thu Nov 02 16:34:00 GMT 2023

REPOSITORIES: MassIVE

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Publications

The human nucleosome acetyltransferase of histone H4 (NuA4)/Tat-interactive protein, 60 kilodalton (TIP60) coactivator complex, a fusion of the yeast switch/sucrose nonfermentable related 1 (SWR1) and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4, H2A, and H2A.Z to regulate gene expression and maintain genome stability. Our cryo-electron microscopy studies show that, within the NuA4/TIP60 complex, the E1A binding protein P400 (EP400) subu  ...[more]

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