Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Crosstalk between combinatorial histone H4 post-translational modifications influence ATAD2B bromodomain activity

ABSTRACT: Investigation of bromodomain activity of the ATPase family which contains ATAD2B. Specifically we explore the cross talk between histone H4 post translational modifications and their modulation of chromatin readers of the ATAD2B bromodomain

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Margaret Phillips

PROVIDER: MSV000091059 | MassIVE | Thu Jan 12 17:35:00 GMT 2023

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Similar Datasets

Crosstalk between combinatorial histone H4 post-translational modifications influence ATAD2B bromodomain activity

Project description:Investigation of bromodomain activity of the ATPase family which contains ATAD2B. Specifically we explore the cross talk between histone H4 post translational modifications and their modulation of chromatin readers of the ATAD2B bromodomain

| MSV000090397 | MassIVE

Crosstalk between combinatorial histone H4 post-translational modifications influence ATAD2B bromodomain activity

| MSV000090384 | MassIVE

Dynamic competing histone H4 K5K8 acetylation and butyrylation are hallmarks of highly active gene promoters

Project description:Newly discovered histone lysine acylations increase the functional diversity of nucleosomes well beyond acetylation. Here, we focus on histone butyrylation in the context of sperm cell differentiation. Specifically, we investigate the butyrylation of histone H4 lysine 5 and 8 at gene promoters, where acetylation guides the binding of Brdt, a bromodomain-and-extra-terminal protein, thereby mediating stage-specific gene expression programs. Genome-wide mapping data show that highly active Brdt-bound gene promoters systematically harbour competing histone acetylation and butyrylation marks at H4 K5 and K8. Histone butyrylation, despite acting as a direct stimulator of transcription, competes with acetylation, especially at H4 K5, to prevent Brdt binding. The observed in vivo H4 K5K8 acetylation butyrylation state at active promoters is reproduced in vitro where p300 indistinctly acetylates and butyrylates H4 K5 and K8. Altogether, highly active gene promoter regions are characterized by alternating H4 acetylation and butyrylation sustaining direct gene activation and a dynamic bromodomain binding.

2016-07-13 | GSE77277 | GEO

Mapping of H4-acetylated chromatin modifications in differentiating human primary myoblasts

Project description:We assessed the genomic distribution of H4-acetylated chromatin by ChIP using SNP chips and an antibody specific to four acetylated lysine residues of H4. Keywords: Comparative genomic hybridization

2006-08-28 | GSE4132 | GEO

Mapping Post-translational Modifications of Histones H2A, H2B and H4 in Schizosaccharomyces pombe.

Project description: Not available

| S-EPMC3079223 | biostudies-literature

Nut is a cell type-specific stimulator of p300 enhancing H4 hyperacetylation during haploid male genome programming

Project description:NUT, nuclear protein in testis is the universal fusion partner of BRD4 in the highly aggressive NUT Midline Carcinoma (NMC), but its physiological function is unknown. Here we show that Nut is exclusively expressed in post-meiotic spermatogenic cells, at the time of genome-wide histone hyperacetylation. Inactivation of Nut induces a spermatogenesis arrest at the histone-to-protamine replacement stage, leading to male infertility. Subsequent molecular investigations show that Nut sustains global histone H4 hyperacetylation in post-meiotic cells. Additionally, Nut mediates a p300/CBP-dependent gene expression program and, by enhancing acetylation of H4 at both K5 and K8 sites, provides binding sites for the first bromodomain of Brdt, which drives histone removal. Our results bring the first evidence of Nut’s function in spermatogenic cells where it uses the ubiquitous HATs p300/CBP to direct a cell-type specific histone H4 hyperacetylation. The ectopic activity of Nut in NMC recreates a forced p300-induced histone hyperacetylation / bromodomain-binding loop that normally operates in post-meiotic spermatogenic cells.

2018-10-15 | GSE111931 | GEO

Rhizobium sp. H4 strain:H4

Project description:Rhizobium sp. H4 strain:H4 Genome sequencing and assembly

| PRJNA433519 | ENA

Post-translational modifications of histones that influence nucleosome dynamics.

Project description: Not available

| S-EPMC4375056 | biostudies-literature

Analysis of Histones H3 and H4 Reveals Novel and Conserved Post-Translational Modifications in Sugarcane.

Project description: Not available

| S-EPMC4520453 | biostudies-literature

Fluctuations in histone H4 isoforms during cellular reprogramming monitored by middle-down proteomics

Project description:Cellular reprogramming remodels the gene expression program by re-setting the epigenome of somatic cells into an embryonic-like state. Post-translational modifications of histones play an important role in this process. We previously used ChIP-seq to profile the distribution of specific histone H3 marks during the entire reprogramming process and found widespread loss of H3K27me3 in the initial stages[1]. Here, using an unbiased middle-down proteomics approach we have identified 74 unique isoforms of histone H4 and quantified them across nine stages of reprogramming. Our data showed substantial differences between the precursor cells and late-phase reprogramming cells. Also, ESCs and iPSCs displayed higher levels of H4 acetylation and tri-methylation concomitantly with lower levels of mono- and di-methylation when compared to cells undergoing reprogramming. These results suggest that during reprogramming, the histone H4 “PTM code” experiences dynamic changes in multiple waves, with a final reset taking place during the transition to an ESC-like state, in perfect agreement with the in-parallel generated multi-omics data[1]. Together, these data represent an invaluable resource to study PTMs of H4 and their potential cross-talk and extend our knowledge on the epigenetic mechanisms involved in acquisition of induced pluripotency.

2015-08-17 | PXD002062 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data