Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability

ABSTRACT: The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability

PROVIDER: PRJNA832341 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR18933100.fastq.gz	Fastqsanger.gz
	SRR18933101.fastq.gz	Fastqsanger.gz
	SRR18933102.fastq.gz	Fastqsanger.gz
	SRR18933103.fastq.gz	Fastqsanger.gz
	SRR18933104.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 62

Similar Datasets

The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability [S1-DRIP-seq]

Project description:Histone chaperones are an important class of factors that regulate chromatin accessibility for DNA-templated processes. Spt6 is a conserved histone chaperone and key regulator of transcription and chromatin structure. However, its functions outside of these roles have been little explored. In this work, we demonstrate a role for Spt6 in DNA replication and more broadly as a regulator of genome stability. Spt6 binds the replication machinery and mutations or loss of Spt6 impair DNA replication in vivo. Additionally, spt6 mutants are sensitive to DNA replication stress inducing agents, with increased sensitivity when combined with loss of DNA replication associated factors. Furthermore, spt6 mutants have elevated levels of DNA double strand breaks and are hyper-recombinogenic. R-loops do not appear to be elevated in spt6 mutants. In total, we identify Spt6 as a regulator of genome stability, at least in part through a role for Spt6 in DNA replication.

2022-04-28 | GSE201633 | GEO

The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability [BrdU-IP-seq]

2022-04-28 | GSE201632 | GEO

The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome stability [MCM ChIPseq]

2023-01-03 | GSE221913 | GEO

The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability [S1-DRIP-seq]

Project description:The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability [S1-DRIP-seq]

| PRJNA832410 | ENA

The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability [BrdU-IP-seq]

Project description:The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability [BrdU-IP-seq]

| PRJNA832411 | ENA

The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome stability [MCM ChIPseq]

Project description:The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome stability [MCM ChIPseq]

| PRJNA916722 | ENA

The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain [ChIP-seq]

Project description:The disassembly and reassembly of nucleosomes by histone chaperones is an essential activity during eukaryotic transcription elongation. This highly conserved process maintains chromatin integrity by transiently removing nucleosomes as barriers and then restoring them in the wake of transcription. While transcription elongation requires multiple histone chaperones, there is little understanding of how most of them function and why so many are required. Here, we show that the histone chaperone Spt6 acts through its acidic, intrinsically disordered N-terminal domain (NTD) to bind histones and control chromatin structure. The Spt6 NTD is essential for viability and its histone binding activity is conserved between yeast and humans. The essential nature of the Spt6 NTD can be bypassed by changes in another histone chaperone, FACT, revealing a close functional connection between the two. Our results have led to a mechanistic model for dynamic cooperation between multiple histone chaperones during transcription elongation.

2024-11-25 | GSE282380 | GEO

The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain [MNase-Seq]

2024-11-25 | GSE282379 | GEO

The conserved histone chaperone Spt6 facilitates DNA replication and mediates genome instability

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

2022-04-28 | GSE201634 | GEO

The histone chaperone Spt6 is required for AID target determination through H3K4me3 regulation

Project description:H3K4me3 plays a critical role in the activation-induced cytidine deaminase (AID)-induced DNA cleavage of switch (S) regions in the immunoglobulin heavy chain (IgH) locus during class-switch recombination (CSR). The histone chaperone complex facilitates chromatin transcription (FACT) is responsible for forming H3K4me3 at AID target loci. Histone chaperone suppressor of Ty6 (Spt6) also participates in regulating H3K4me3 for CSR and for somatic hypermutation (SHM) in AID target loci. H3K4me3 loss was correlated with defects in AID-induced DNA breakage and reduced mutation frequencies in IgH loci, in both S and variable regions, and in non-IgH loci, such as metastasis-associated lung adenocarcinoma transcript 1 (MALAT1) and small nucleolar RNA host gene 3 (SNHG3). Global gene expression analysis revealed that Spt6 can act as both a positive and negative transcriptional regulator in B cells, affecting approximately 5% of the genes that includes suppressor of Ty4 (Spt4) and AID. Interestingly, Spt6 regulates CSR and AID expression through two distinct histone modification pathways, H3K4me3 and H3K36me3, respectively. Spt6 is a unique histone chaperone, capable of regulating the histone epigenetic state of both AID targets and the AID locus. CH12F3-2A cells were transfected with control and Spt6 siRNAs; 24h later, cells were stimulated with CIT to induce CSR. Total RNA was extracted from control and Spt6 siRNA treated cells for mRNA expression profiling.

2013-02-01 | E-GEOD-35334 | biostudies-arrayexpress

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