Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Drosophila SWR1 and NuA4 complexes originate from DOMINO splice isoforms

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

OTHER RELATED OMICS DATASETS IN: PXD017729

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE145738 | GEO | 2020/05/19

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Similar Datasets

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 are defined by DOMINO isoforms.

Project description: Not available

| S-EPMC7239659 | biostudies-literature

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

| PRJNA608023 | ENA

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

Swc4 positively regulates telomere length independently of its roles in NuA4 and SWR1 complexes.

Project description: Not available

| S-EPMC7736797 | biostudies-literature

Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain.

Project description: Not available

| S-EPMC5758897 | biostudies-literature

Isw1 functions in parallel with the NuA4 and Swr1 complexes in stress-induced gene repression.

Project description: Not available

| S-EPMC1592817 | biostudies-literature