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The histone demethylase JMJ27 acts during the UV-induced modulation of H3K9me2 landscape and facilitates photodamage repair

ABSTRACT: The histone demethylase JMJ27 acts during the UV-induced modulation of H3K9me2 landscape and facilitates photodamage repair

PROVIDER: PRJNA1098035 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28599200.fastq.gz	Fastqsanger.gz
	SRR28599201.fastq.gz	Fastqsanger.gz
	SRR28599202.fastq.gz	Fastqsanger.gz
	SRR28599203.fastq.gz	Fastqsanger.gz
	SRR28599204.fastq.gz	Fastqsanger.gz

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The histone demethylase JMJ27 acts during the UV-induced modulation of H3K9me2 landscape and facilitates photodamage repair

Project description:We used ChIP-seq to identify changes in H3K9me2 contents upon UV-C exposure in WT Arabidopsis plants and in plants deficient for the expression of the histone demethylase, Jumonji27 (JMJ27)

2024-09-05 | GSE263549 | GEO

Photodamage repair pathways contribute to the accurate maintenance of DNA methylome landscape upon UV exposure

Project description:We report the methylation level of photodamage repair deficient plants 24h upon UV-C exposure. We determined the methlome changes genome wide and at photodamaged sites using NGS approaches.

2019-11-01 | GSE132750 | GEO

α-Arbutin Prevents UVA-Induced Skin Photodamage via Alleviating DNA Damage and Collagen Degradation in NIH-3T3 cells

Project description:Ultraviolet radiation (UV) causes certain side effects to the skin, and their accumulation to a certain extent can lead to accelerated aging of the skin. Recent studies suggests that α-arbutin may be useful in various disorders such as hyperpigmentation disorders, wound healing, and antioxidant activity. However, the role of α-arbutin in skin photodamage is unclear. In this study, under UVA-induced photodamage conditions, α-arbutin treated mouse skin fibroblasts (NIH-3T3) can repair DNA damage and resist apoptosis by reducing the production of reactive oxygen species (ROS) and increasing the phosphorylation of glycogen synthase kinase 3 beta (GSK3β) to orchestra AKT/GSK3β pathway. Meanwhile, α-arbutin can also regulate collagen metabolism and facilitate the replenishment of collagen by targeting the phosphorylation of SMAD3 to mediate the TGFβ/SMAD pathway in NIH-3T3. In conclusion, we found that α-arbutin can mitigate the detrimental effects of skin photodamage induced by UVA irradiation, and provides a theoretical basis for the use of α-arbutin in the treatment of skin photodamage.

2025-06-01 | GSE281390 | GEO

Photodamage repair pathways contribute to the accurate maintenance of DNA methylome landscape upon UV exposure

Project description:Photodamage repair pathways contribute to the accurate maintenance of DNA methylome landscape upon UV exposure

| PRJNA548919 | ENA

MBD8 is required for LDL2-mediated transcriptional repression downstream of H3K9me2 in Arabidopsis

Project description:Histone H3 lysine 9 methylation (H3K9me) is a conserved epigenetic mark for transcriptional gene repression. In Arabidopsis, H3K9 dimethylation (H3K9me2) promotes the removal of a transcription-associated mark, H3K4 monomethylation (H3K4me1), and this process within genes requires the histone demethylase LDL2. However, how LDL2 specifically functions in genes that accumulate H3K9me2 remains unknown. Here, we show that methyl-CpG-binding domain protein 8 (MBD8) binds to LDL2 and plays a role in H3K4me1 removal and transcriptional gene repression downstream of H3K9me2. MBD8 preferentially binds GC-poor DNA, regardless of its cytosine methylation status. Interestingly, LDL2 protein levels were significantly reduced in the mbd8 mutant background, suggesting that MBD8 stabilizes the LDL2 protein, facilitating H3K4me1 removal and the transcriptional repression of H3K9me-marked genes. The domain necessary for the MBD8-LDL2 interaction is conserved among plants. We propose that MBD proteins have diverse functions beyond their methylated DNA-binding capabilities.

2026-06-08 | PXD069014 | Pride

To better understand the molecular basis for modulation of glycosaminoglycans (GAGs) and proteoglycans post-UV exposure

Project description:UV irradiation is a major environmental effector of skin damage and aging. Elevated levels of glycosaminoglycans (GAGs), as measured by Hale’s stain, are seen following cutaneous photodamage. Preliminary data from our lab indicates that this is a complex response involving differential regulation of both GAGs and proteoglycans. Recently, different GAG species have been shown to have distinct effects on the recruitment and activation of immune cells and stimulation of cytokine production (Taylor and Gallo, FASEB, 2006; 20: 9-22). We speculate that the elevated GAGs and proteoglycans observed after ultraviolet B (UVB) irradiation are involved in the inflammatory and healing responses to photodamage.

2011-10-03 | GSE32552 | GEO

Protective Effect of Ginsenoside Re against UVB-Induced Photodamage in Rats

Project description:Background: With the growing prominence of skin photodamage caused by ultraviolet (UV) radiation, the development of efficient and safe natural photoprotectants has become a major research focus. Ginsenoside Re, a rare active component of Panax ginseng, has attracted much attention due to its significant antioxidant and anti-inflammatory activities, but its systemic role and mechanism in protecting against photodamage remain unclear.  Objective: To exploring the mechanism behind the therapeutic effect of Re on UVB-Induced skin photodamage in a rat model Methods: In this study, a UVB-induced rat photodamage model was established to evaluate the protective effect of ginsenoside Re through histopathological staining, biochemical index detection, etc. and combined with transcriptome and metabolomics analysis to screen differentially expressed genes and metabolites, thereby revealing metabolic pathways and gene functions associated with the photodamage phenotype. Key targets were further verified through multi-omics integration and Western blotting.Results: The results showed that ginsenoside Re could effectively alleviate UVB-induced pathological injury of skin tissue, reduce the level of oxidative stress and the release of inflammatory factors. In addition, it could effectively reverse the abnormal expression of 265 differential genes and 30 metabolites. Through multi-omics association analysis and WB verification, the glutathione metabolism pathway was identified as a key pathway mediating the protective effects of ginsenoside Re against skin photodamage.

2025-10-16 | MTBLS13149 | MetaboLights

m6A directs the demethylation of histone H3K9me2 co-transcriptionall

Project description:Here we show the repressive H3K9me2 mark is specifically removed by the induction of m6A-modified transcripts. We demonstrate that the methyltransferase METTL3/METTL14 regulates H3K9me2 modification. We observed a genome-wide correlation between m6A and occupancy by the H3K9me2 demethylase KDM3B, and we found m6A reader YTHDC1 physically interacts and recruits KDM3B to m6A-associated chromatin regions, promoting H3K9me2 demethylation and gene expression. This study establishes a direct link between m6A and dynamic chromatin modification and provides mechanistic insight into the co-transcriptional interplay between RNA modification and histone modifications.

2020-07-01 | GSE153651 | GEO

Effect of loss of Jmjd1c on H3K9me2 level across the genome

Project description:Analysis of H3K9me2 level in MLL-AF9 leukemia cells upon deletion of Jmjd1c. Jmjd1c has been shown to be a H3K9me1/2 demethylase and these results provide insight into its role in MLL-Af9 leukemia

2016-06-09 | GSE75577 | GEO

Plant homeodomain targeting cyclic peptides allosterically modulate KDM7 histone demethylase activity

Project description:Here we report the discovery of a set of potent de-novo cyclic peptides (CPs) targeting different binding sites on KDM7B. One CP (OC9) bound directly to the KDM7 PHD-finger, as supported by bio-layer interferometry (BLI), isothermal calorimetry (ITC), hydrogen-deuterium exchange mass spectrometry (HDxMS) and NMR studies, and was highly selective for KDM7s over other PHD-fingers. OC9 disrupted PHD-finger binding to H3K4me3, and allosterically modulated KDM7 demethylase activity at H3K9me2 site on peptides and histone extracts demonstrating PHD-finger targeting is as JmjC-domain targeted inhibitors, but more selective for specific KDM7 subfamily member and certain combinatorial histone PTM signatures. Proteomic analysis confirmed OC9 to selectively target KDM7 in nuclear lysates demonstrating its high affinity and selectivity against other H3K4me3 reader domains and KDMs.

2023-07-20 | PXD027151 | Pride

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