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

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE261652 | GEO | 2024/08/06

REPOSITORIES: GEO

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

Project description: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.

2024-08-08 | PXD053209 | Pride

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

Project description: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.

2024-08-08 | PXD053207 | Pride

Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [RNA-seq]

2024-08-06 | GSE261651 | GEO

Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [ChIP-seq]

2024-08-06 | GSE261650 | GEO

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

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

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Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [ChIP-seq]

Project description:Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [ChIP-seq]

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Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [RNA-seq]

Project description:Unique structural features of the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex [RNA-seq]

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ZMYND11-MBTD1 induces leukemogenesis through hijacking NuA4/TIP60 acetyltransferase complex and a PWWP-mediated chromatin association mechanism.

Project description:Recurring chromosomal translocation t(10;17)(p15;q21) present in a subset of human acute myeloid leukemia (AML) patients creates an aberrant fusion gene termed ZMYND11-MBTD1 (ZM); however, its function remains undetermined. Here, we show that ZM confers primary murine hematopoietic stem/progenitor cells indefinite self-renewal capability ex vivo and causes AML in vivo. Genomics profilings reveal that ZM directly binds to and maintains high expression of pro-leukemic genes including Hoxa, Meis1, Myb, Myc and Sox4. Mechanistically, ZM recruits the NuA4/Tip60 histone acetyltransferase complex to cis-regulatory elements, sustaining an active chromatin state enriched in histone acetylation and devoid of repressive histone marks. Systematic mutagenesis of ZM demonstrates essential requirements of Tip60 interaction and an H3K36me3-binding PWWP (Pro-Trp-Trp-Pro) domain for oncogenesis. Inhibitor of histone acetylation-'reading' bromodomain proteins, which act downstream of ZM, is efficacious in treating ZM-induced AML. Collectively, this study demonstrates AML-causing effects of ZM, examines its gene-regulatory roles, and reports an attractive mechanism-guided therapeutic strategy.

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MYC recruits the TIP60 histone acetyltransferase complex to chromatin.

Project description:The transcription factor MYC binds specific DNA sites in cellular chromatin and induces the acetylation of histones H3 and H4. However, the histone acetyltransferases (HATs) that are responsible for these modifications have not yet been identified. MYC associates with TRRAP, a subunit of distinct macromolecular complexes that contain the HATs GCN5/PCAF or TIP60. Although the association of MYC with GCN5 has been shown, its interaction with TIP60 has never been analysed. Here, we show that MYC associates with TIP60 and recruits it to chromatin in vivo with four other components of the TIP60 complex: TRRAP, p400, TIP48 and TIP49. Overexpression of enzymatically inactive TIP60 delays the MYC-induced acetylation of histone H4, and also reduces the level of MYC binding to chromatin. Thus, the TIP60 HAT complex is recruited to MYC-target genes and, probably with other other HATs, contributes to histone acetylation in response to mitogenic signals.

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Gene-specific RNA homeostasis revealed by perturbation of the NuA4/Tip60 acetyltransferase complex

Project description:This SuperSeries is composed of the SubSeries listed below.

2024-01-30 | GSE253313 | GEO