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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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Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms

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

| PRJNA608021 | ENA

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]

| PRJNA606578 | ENA

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.

2020-05-19 | GSE145737 | GEO

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

2020-05-19 | GSE145269 | GEO

Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms

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

2020-05-19 | GSE145738 | GEO

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: Not available

| S-EPMC7239659 | biostudies-literature

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

Project description:The histone variant H2A.Z is a genome-wide signature of nucleosomes proximal to eukaryotic regulatory DNA. While the multi-subunit SWR1 chromatin remodeling complex is known to catalyze ATP-dependent deposition of H2A.Z, the mechanism of recruitment to S. cerevisiae promoters has been unclear. A sensitive assay for competitive binding of di-nucleosome substrates revealed that SWR1 preferentially binds long nucleosome-free DNA adjoining core particles, allowing discrimination of gene promoters over gene bodies. We traced the critical DNA binding component of SWR1 to the conserved Swc2/YL1 subunit, whose activity is required for both SWR1 binding and H2A.Z incorporation in vivo. Histone acetylation by NuA4 enhances SWR1 binding, but the interaction with nucleosome-free DNA is the major determinant. ‘Hierarchical cooperation’ between high affinity DNA- and low affinity histone modification-binding factors may reconcile the large disparity in affinities for chromatin substrates, and unify classical control by DNA-binding factors with post-translational histone modifications and ATP-dependent nucleosome mobility. Swr1 TAP IF of various mutants

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

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

2013-09-16 | GSE49183 | GEO

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