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Investigating how the SPT2 histone chaperone affects chromatin structure in human osteosarcoma cells.

ABSTRACT: Investigating how the SPT2 histone chaperone affects chromatin structure in human osteosarcoma cells.

PROVIDER: PRJNA1017514 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26065300_1.fastq.gz	Fastqsanger.gz
	SRR26065300_2.fastq.gz	Fastqsanger.gz
	SRR26065301_1.fastq.gz	Fastqsanger.gz
	SRR26065301_2.fastq.gz	Fastqsanger.gz
	SRR26065302_1.fastq.gz	Fastqsanger.gz

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Investigating how the SPT2 histone chaperone affects chromatin structure in human osteosarcoma cells.

Project description:Histone chaperones play essential roles in the regulation of chromatin structure. Here, we investigated how the SPT2 histone chaperone controls chromatin structure and accessibility in human cells (using U-2 OS osteosarcoma cells as model; these cells also express a H3.3-SNAP transgene). To achieve this, we performed ATAC-seq comparing WT U2OS vs three independent SPT2 KO clones (KO-3, KO-4 and KO-6

2023-09-15 | GSE243274 | GEO

Investigating how the SPT-2 histone chaperone affects chromatin structure in C. elegans.

Project description:Investigating how the SPT-2 histone chaperone affects chromatin structure in C. elegans.

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Investigating how the SPT-2 histone chaperone affects chromatin structure in C. elegans.

Project description:Histone chaperones play essential roles in the regulation of chromatin structure. Here, we investigated how the SPT-2 histone chaperone controls chromatin structure and accessibility in C. elegans. To achieve this, we performed ATAC-seq comparing WT N2 worms to spt-2 KO or spt-2 histone binding mutant (spt-2 M627A) worms.

2023-02-09 | GSE224799 | GEO

Structure of the Hir histone chaperone complex

Project description:The evolutionarily conserved HIRA/Hir histone chaperone complex and ASF1/Asf1 co-chaperone cooperate for replication-independent chromatin assembly. Here we report the molecular architecture of the Hir complex with Asf1/H3/H4 via single-particle cryo-EM and crosslinking mass spectrometry.

2024-08-22 | PXD040705 | Pride

Investigating how the loss of RelB affects RelA DNA binding [ChIP-seq]

Project description:Investigating how the loss of RelB affects RelA DNA binding [ChIP-seq]

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Genome-wide maps of histone H2A.Z and its chaperone.

Project description:We use ChIP-Seq technology to profile the occupancy of histone H2A.Z and its chaperone in HeLa cells genome wide to check if they are co-colocalized. H2A.Z is ChIPed by antibody and its chaperone is tagged by Flag and ChIPed by M2 beads against Flag. ChIPed fragments are sequenced by Illumina HiSeq 2000 platform.

2014-03-01 | E-GEOD-52371 | biostudies-arrayexpress

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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.

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

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IDO1 overexpression significantly affects exosomal miRNA subsets derived from osteosarcoma and ordinary osteoblasts

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DNAJC9 Integrates Heat Shock Molecular Chaperones into the Histone Chaperone Network

Project description:From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize a histone chaperone function of DNAJC9, a heat shock co-chaperone that promotes HSP70-mediated catalysis. We elucidate the structure of DNAJC9, in a histone H3-H4 co-chaperone complex with MCM2, revealing how this dual histone and heat shock co-chaperone binds histone substrates. We show that DNAJC9 recruits HSP70-type enzymes via its J domain to fold histone H3-H4 substrates: upstream in the histone supply chain, during replication- and transcription-coupled nucleosome assembly, and to clean up spurious interactions. With its dual functionality, DNAJC9 integrates ATP-resourced protein folding into the histone supply pathway to resolve aberrant intermediates throughout the dynamic lives of histones.

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