Proteomics

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Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Jie Luo  

LAB HEAD: Jeff Ranish

PROVIDER: PXD053209 | Pride | 2024-08-08

REPOSITORIES: Pride

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Dataset's files

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Action DRS
JL031824_031924_P400_NCP_1ug.mzXML Mzxml
JL031824_031924_P400_NCP_RP1.mzXML Mzxml
JL031824_031924_P400_NCP_RP10.mzXML Mzxml
JL031824_031924_P400_NCP_RP2.mzXML Mzxml
JL031824_031924_P400_NCP_RP3.mzXML Mzxml
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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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