Methyl-CpG-binding domain (MBD) sequencing of neuroblastoma tumors
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA285076 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR2040290_1.fastq.gz | Fastqsanger.gz | |||
| SRR2040290_2.fastq.gz | Fastqsanger.gz | |||
| SRR2040300_1.fastq.gz | Fastqsanger.gz | |||
| SRR2040300_2.fastq.gz | Fastqsanger.gz | |||
| SRR2040310_1.fastq.gz | Fastqsanger.gz |
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Project description:The DNA methylome of 45 primary neuroblastoma tumors is profiled by enrichment with a methyl-CpG-binding domain (MBD) and massively parallel sequencing DNA of 45 primary tumors is sheared (fragments of ± 200 bp), followed by MBD-based (MethylCap kit of Diagenode) enrichement, library preparation and multiplexing. Both input DNA and captured DNA were sequenced paired-end on Illumina Hiseq2000
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Project description:The DNA methylome of 15 primary stage 4S neuroblastoma tumors is profiled by enrichment with a methyl-CpG-binding domain (MBD) and massively parallel sequencing DNA of 15 primary stage 4S tumors is sheared (fragments of ± 200 bp), followed by MBD-based (MethylCap kit of Diagenode) enrichement, library preparation and multiplexing. Both input DNA and captured DNA were sequenced paired-end on Illumina Hiseq2000
2015-12-15 | E-GEOD-69268 | biostudies-arrayexpress
Project description:The repressive capacity of cytosine DNA methylation is mediated by recruitment of silencing complexes by methyl-CpG binding domain (MBD) proteins. Unexpectedly, we discovered that a family of arthropod Copia retrotransposons have incorporated a host-derived MBD domain. We functionally demonstrate how retrotransposon encoded MBDs preferentially bind to CpG-dense methylated regions, which correspond to transposable element regions of the host genome, in the myriapod Strigamia maritima. Consistently, young MBD-encoding Copia retrotransposons (CopiaMBD) accumulate in regions with higher CpG-densities than other LTR-retrotransposons also present in the genome. This would suggest that retrotransposons use MBDs to integrate into heterochromatic regions in Strigamia, avoiding potentially harmful insertions into host genes. In contrast, CopiaMBD insertions in the spider Stegodyphus dumicola genome disproportionately accumulate in methylated gene bodies when compared to other spider LTR-retrotransposons. Given that transposons are not actively targeted by DNA methylation in the spider genome, this distribution bias would also support a role for MBDs in the integration process. Together, these data demonstrate that retrotransposons can co-opt host-derived epigenome readers, potentially harnessing the host epigenome landscape to advantageously tune the retrotransposition process.
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Project description:Methyl-CpG binding domain protein sequencing (MBD-seq) for three kinds of chick germ cells Genome sequencing
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Project description:Methyl CpG binding domain 3 (Mbd3) protein belongs to the MBD family of proteins, responsible for reading the DNA methylation pattern. MBD family proteins bind the methyl-CpG domain and are also involved in heterochromatin formation. Mbd3 protein does not have the ability to selectively recognize methyl-CpG islands, however, its characteristic feature is the ability to bind to 5-hydroxymethylcytosine and unmethylated DNA. Little is known about the role of Mbd3 in epilepsy and epileptogenesis. Our previous study (Bednarczyk et al., 2016) showed an increase in levels of NuRD complex proteins, including Mbd3 protein, in the brain of epileptic animals in a rat model of temporal epilepsy induced by electrical stimulation of the amygdala. Amygdala stimulation induced the binding of NuRD complex containing MBD3 to larger number of regions of DNA. In the present study, we investigated whether the Mbd3 protein is involved in the determination of the seizure threshold. An increase in Mbd3 protein levels was demonstrated in the entorhinal cortex/amygdala in the rat’s brain 4 hours after pentylenetetrazole (PTZ)-induced seizures. No alterations in MBD3 protein levels were detected in hippocampus and somatosensory cortex. No alterations in MBD3 mRNA expression were observed at any time point in any studied brain area. Reduction of Mbd3 level using AAV vector coding shRNA against Mbd3 injected to the amygdala prolonged the latency time to the onset of an acute seizure in PTZ challenge test indicating increase in seizure threshold. This was accompanied by increased anxiety in the open field test. In the contrast, an overexpression of Mbd3 using AAV decreased anxiety and increased their excitability in the open field test. Moreover Mbd3 overexpression in the amygdala accelerated epileptogenesis in the PTZ-kindling model. In order to identify the role of Mbd3 protein in the regulation of gene expression, mRNA profiling with RNA-seq was performed in a model of magnesium deficiency-induced epileptiform discharges in vitro. Mbd3 overexpression in vitro induced changes in gene expression in a time- and state-specific manner. Our data indicate the pro-epileptic properties of the Mbd3 protein in vivo and in vitro.
2024-02-09 | GSE227084 | GEO
Project description:In order to gain insight into DNA methylation readout, we have established a controlled strategy for profiling genomic targeting of chromatin-interacting factors in vivo. With this approach we determined binding preferences for the methyl-CpG binding domain (MBD) family of proteins, including disease relevant mutants, deletions and isoforms. In vivo binding of MBD proteins occurs as a linear function of local methylation density, and is dependent on functional MBD domain – methyl-CpG interactions. This directs specificity of MBD proteins to methylated, CpG dense and inactive regulatory regions. In contrast, binding to unmethylated sites is MBD protein specific and mediated via alternative domains or protein-protein interactions. The latter is observed for NuRD complex-mediated MBD2 tethering to a subset of unmethylated, tissue-specific regulatory regions, similar to MBD3. These functional binding maps reveal methylation-dependent and -independent binding modes determined by distinct protein domains and revise current models of DNA methylation readout through MBD proteins.
2013-04-01 | GSE39610 | GEO
Project description:In order to gain insight into DNA methylation readout, we have established a controlled strategy for profiling genomic targeting of chromatin-interacting factors in vivo. With this approach we determined binding preferences for the methyl-CpG binding domain (MBD) family of proteins, including disease relevant mutants, deletions and isoforms. In vivo binding of MBD proteins occurs as a linear function of local methylation density, and is dependent on functional MBD domain M-bM-^@M-^S methyl-CpG interactions. This directs specificity of MBD proteins to methylated, CpG dense and inactive regulatory regions. In contrast, binding to unmethylated sites is MBD protein specific and mediated via alternative domains or protein-protein interactions. The latter is observed for NuRD complex-mediated MBD2 tethering to a subset of unmethylated, tissue-specific regulatory regions, similar to MBD3. These functional binding maps reveal methylation-dependent and -independent binding modes determined by distinct protein domains and revise current models of DNA methylation readout through MBD proteins. Comparative binding analysis for the MBD family of proteins utilizing recombinase-assisted mapping of biotin-tagged proteins (RAMBiO). This set contains maps for 29 samples including wild type MBD proteins, mutants and domain variants in mouse ES cells, derived neurons (NP and TN) and Dnmt1/3a/3b triple-KO ES cells (TKO).
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