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Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms [ChIP-seq]

ABSTRACT: Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms [ChIP-seq]

PROVIDER: PRJNA608023 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11143800.fastq.gz	Fastqsanger.gz
	SRR11143801.fastq.gz	Fastqsanger.gz
	SRR11143802.fastq.gz	Fastqsanger.gz
	SRR11143803.fastq.gz	Fastqsanger.gz
	SRR11143804.fastq.gz	Fastqsanger.gz

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Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms

Project description:Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms

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Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms [RNA-seq]

Project description:Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms [RNA-seq]

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Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms [ChIP-seq]

Project description:Histone acetylation and deposition of H2A.Z variant are integral aspects of active transcription. In Drosophila, the single DOMINO chromatin regulator complex is thought to combine both activities via an unknown mechanism. Here we show that two alternative splice isoforms of the DOMINO nucleosome remodeling ATPase, DOM-A and DOM-B, directly specify two distinct multi-subunit complexes. Both complexes are necessary for transcriptional regulation but through different mechanisms. The DOM-B complex incorporates H2A.V (the fly ortholog of H2A.Z) genome-wide in an ATP-dependent manner, like the yeast SWR1 complex. The DOM-A complex, instead, functions as an ATP-independent histone acetyltransferase complex similar to the yeast NuA4, targeting lysine 12 of histone H4. Our work provides an instructive example of how different evolutionary strategies lead to similar functional separation.

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Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms [RNA-seq]

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Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms

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

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NuA4 and SWR1 complex in Plasmodium falciparum

Project description: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, in P. falciparum.

2024-03-18 | PXD046547 | Pride

Drosophila SWR1 and NuA4 complexes are defined by DOMINO isoform

Project description: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 ATPase, DOM-A and DOM-B, directly specify two distinct multi-subunit complexes. Both complexes are necessary for transcriptional regulation but through different mechanisms. The DOM-B complex incorporates H2A.V (the fly ortholog of H2A.Z) genome-wide in an ATP-dependent manner, like the yeast SWR1 complex. The DOM-A complex, instead, functions as an ATP-independent histone acetyltransferase com-plex similar to the yeast NuA4, targeting lysine 12 of histone H4. Our work provides an in-structive example of how different evolutionary strategies lead to similar functional separation. In yeast and humans, nucleosome remodeling and histone acetyltransferase complexes orig-inate from gene duplication and paralog specification. Drosophila generates the same diversi-ty by alternative splicing of a single gene.

2020-05-27 | PXD017729 | Pride

Drosophila SWR1 and NuA4 complexes are defined by DOMINO isoforms.

Project description:Histone acetylation and deposition of H2A.Z variant are integral aspects of active transcription. 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 ATPase, DOM-A and DOM-B, directly specify two distinct multi-subunit complexes. Both complexes are necessary for transcriptional regulation but through different mechanisms. The DOM-B complex incorporates H2A.V (the fly ortholog of H2A.Z) genome-wide in an ATP-dependent manner, like the yeast SWR1 complex. The DOM-A complex, instead, functions as an ATP-independent histone acetyltransferase complex similar to the yeast NuA4, targeting lysine 12 of histone H4. Our work provides an instructive example of how different evolutionary strategies lead to similar functional separation. In yeast and humans, nucleosome remodeling and histone acetyltransferase complexes originate from gene duplication and paralog specification. Drosophila generates the same diversity by alternative splicing of a single gene.

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Nucleosome free DNA- and acetyl histone-binding components recruit SWR1 to yeast promoters for H2A.Z replacement

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2013-09-16 | E-GEOD-49183 | biostudies-arrayexpress

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.

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