Dataset Information

Crosslinking mass spectrometry of DDM1 complexed with the nucleosome

ABSTRACT: DECREASE IN DNA METHYLATION 1 (DDM1) is the chromatin remodeling factor that has been genetically identified in Arabidopsis thaliana as a factor involved in the maintenance of repressive epigenomic modifications over transposons. In this study, we performed crosslinking mass spectrometry and biochemical analysis using reconstituted nucleosome to understand the chromatin remodeling activity of DDM1. We found that the unique C-terminal tail of heterochromain-specific H2A.W variant binds to DDM1. This result suggest that DDM1 functions with specific histone variants for the maintenance of repressive modifications and epigenetic regulation of transposon activity.

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Hitoshi Kurumizaka, Akihisa Osakabe

PROVIDER: PXD043417 | JPOST Repository | Fri May 31 00:00:00 BST 2024

REPOSITORIES: jPOST

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			Action	DRS
	DDM1H2AW_221125osad20_1117F60XL_2ul.raw	Raw
	DDM1H2AW_221125osad21_1117F60XL_2ul.raw	Raw
	DDM1H2A_221125osab00_1117F60XL_2ul.raw	Raw
	DDM1H2A_221125osab06_1117F60XL_2ul.raw	Raw
	DDM1H2A_221125osab07_1117F60XL_2ul.raw	Raw

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Project description:Histone modifications associated with gene silencing typically mark large contiguous regions of the genome forming repressive chromatin domain structures. Since the repressive domains exist in close proximity to active regions, maintenance of domain structure is critically important. This study shows that nickel, a nonmutagenic carcinogen, can disrupt histone H3 lysine 9 dimethylation (H3K9me2) domain structures genome-wide, resulting in spreading of H3K9me2 marks into the active regions, which is associated with gene silencing. Our results suggest inhibition of DNA binding of the insulator protein CCCTC-binding factor (CTCF) at the H3K9me2 domain boundaries as a potential reason for H3K9me2 domain disruption. These findings have major implications in understanding chromatin dynamics and the consequences of chromatin domain disruption during pathogenesis. Investigations into the genomic landscape of histone modifications in heterochromatic regions have revealed histone H3 lysine 9 dimethylation (H3K9me2) to be important for differentiation and maintaining cell identity. H3K9me2 is associated with gene silencing and is organized into large repressive domains that exist in close proximity to active genes, indicating the importance of maintenance of proper domain structure. Here we show that nickel, a nonmutagenic environmental carcinogen, disrupted H3K9me2 domains, resulting in the spreading of H3K9me2 into active regions, which was associated with gene silencing. We found weak CCCTC-binding factor (CTCF)-binding sites and reduced CTCF binding at the Ni-disrupted H3K9me2 domain boundaries, suggesting a loss of CTCF-mediated insulation function as a potential reason for domain disruption and spreading. We furthermore show that euchromatin islands, local regions of active chromatin within large H3K9me2 domains, can protect genes from H3K9me2-spreadingM-bM-^@M-^Sassociated gene silencing. These results have major implications in understanding H3K9me2 dynamics and the consequences of chromatin domain disruption during pathogenesis.