Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation [CUT&Run_2]

ABSTRACT: We profiled H4K20 monomethylation and KMT5A during the well-characterized erythroid differentiation of human hematopoietic stem and progenitor cells.

ORGANISM(S): Homo sapiens

PROVIDER: GSE300158 | GEO | 2025/07/30

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&Tag)

Project description:We profiled H4K20 mono- and tri- methylation during the well-characterized erythroid differentiation of human hematopoietic stem and progenitor cells.

2025-07-30 | GSE260721 | GEO

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&RUN)

Project description:We profiled H4K20 mono- and tri- methylation during the well-characterized erythroid differentiation of human hematopoietic stem and progenitor cells.

2025-07-30 | GSE260720 | GEO

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation

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

2025-07-30 | GSE260722 | GEO

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation

Project description:Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation

| PRJNA1082771 | ENA

Methylation of histone H4 lysine 20 by PR-Set7 ensures the integrity of late replicating sequence domains in Drosophila

Project description:The methylation state of lysine 20 on histone H4 (H4K20) has been linked to cell cycle progression, Origin Recognition Complex (ORC) binding, and replication origin regulation. Monomethylation of H4K20 (H4K20me1) is mediated by the cell cycle-regulated histone methyltransferase PR-Set7, which is essential for genome integrity and cell cycle progression. PR-Set7 depletion in mammalian cells results in defective S-phase progression and the accumulation of DNA damage, which could be partially attributed to a defect in pre-Replication Complex (pre-RC) formation and origin activity. However, these studies were limited to a handful of mammalian origins, and it remains unclear how PR-Set7 and H4K20 methylation impact the replication program on a genomic scale. Using Drosophila Kc167 cells, we employed genetic, cytological, and genomic approaches to better understand the role of PR-Set7 and H4K20 methylation in regulating DNA replication and governing genome stability. We find that depletion of Drosophila PR-Set7 and loss of H4K20me1 result in the accumulation of DNA damage and an ATR-dependent cell cycle arrest. The cell cycle arrest occurs during the second S-phase following loss of PR-Set7 activity, suggesting that accumulation of nascent H4K20 is recalcitrant to the DNA replication program. Deregulation of H4K20 methylation had no impact on origin activation throughout the genome; instead, we found that the DNA damage marker, phosphorylated H2A.v (γ-H2A.v), accumulated specifically in late replicating domains in the absence of PR-Set7. This suggests that the molecular basis for the cell cycle arrest and accumulation of DNA damage resulting from loss of PR-Set7 is stochastic fork collapse within late replicating domains.

2015-10-08 | GSE73668 | GEO

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&RUN)

Project description:Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&RUN)

| PRJNA1082773 | ENA

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&Tag)

Project description:Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation (CUT&Tag)

| PRJNA1082774 | ENA

Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation [CUT&Run_2]

Project description:Histone H4 Lysine 20 Methylation Marks Genes Dynamically Regulated During Erythroid Maturation [CUT&Run_2]

| PRJNA1279139 | ENA

Histone lysine methyltransferase Pr-set7/SETD8 promotes neural stem cell reactivation

Project description:The ability of neural stem cells (NSCs) to switch between quiescence and proliferation is crucial for brain development and homeostasis. Increasing evidence suggest that variants of histone lysine methyltransferases including KMT5A are associated with neurodevelopmental disorders. However, the function of KMT5A/Pr-set7/SETD8 in the central nervous system is not well established. Here, we show that Drosophila Pr-Set7 is a novel regulator of NSC reactivation. Loss-of-function of pr-set7 causes a delay in NSC reactivation and loss of H4K20 monomethylation in the brain. Through NSC-specific in vivo profiling, we demonstrate that Pr-set7 binds to the promoter region of cyclin dependent kinase 1 (cdk1) and Wnt pathway transcriptional co-activator earthbound1/jerky (ebd1). Further validation indicates that Pr-set7 is required for the expression of cdk1 and ebd1 in the brain. Similar to Pr-set7, Cdk1 and Ebd1 promote NSC reactivation. Moreover, Cdk1 upregulates the Ebd1 levels in NSCs, while Ebd1 appears to downregulate Cdk1 expression, suggesting a negative feedback regulation. Finally, overexpression of Cdk1 and Ebd1 significantly suppressed NSC reactivation defects observed in pr-set7-depleted brains. Therefore, Pr-set7, the sole H4K20 methyltransferase, promotes NSC reactivation through regulating Wnt signaling and cell-cycle progression. Given the conservation of Pr-set7, our findings may contribute to the understanding of mammalian KMT5A/PR-SET7/SETD8 in NSC proliferation and associated neurodevelopmental disorders.

2021-02-09 | GSE158764 | GEO

Preferential dimethylation of histone H4 lysine 20 by Suv4-20.

Project description:Post-translational modifications of histone tails direct nuclear processes including transcription, DNA repair, and chromatin packaging. Lysine 20 of histone H4 is mono-, di-, or trimethylated in vivo, but the regulation and significance of these methylations is poorly understood. The SET domain proteins PR-Set7 and Suv4-20 have been implicated in mono- and trimethylation, respectively; however, enzymes that dimethylate lysine 20 have not been identified. Here we report that Drosophila Suv4-20 is a mixed product specificity methyltransferase that dimethylates approximately 90% and trimethylates less than 5% of total H4 at lysine 20 in S2 cells. Trimethylation, but not dimethylation, is reduced in Drosophila larvae lacking HP1, suggesting that an interaction with HP1 regulates the product specificity of Suv4-20 and enrichment of trimethyllysine 20 within heterochromatin. Similar to the Drosophila enzyme, human Suv4-20h1/h2 enzymes generate di- and trimethyllysine 20. PR-Set7 and Suv4-20 are both required for normal levels of methylation, suggesting they have non-redundant functions. Alterations in the level of lysine 20 methylation following knock-down or overexpression of Suv4-20 did not affect lysine 16 acetylation, revealing that these two modifications are not competitive in vivo. Depletion of Suv4-20h1/h2 in HeLa cells impaired the formation of 53BP1 foci, suggesting dimethyllysine 20 is required for a proper DNA damage response. Collectively, the data indicate that Suv4-20 generates nearly ubiquitous dimethylation that facilitates the DNA damage response and selective trimethylation that is involved in heterochromatin formation.

| S-EPMC2335358 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

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