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Linking DNA Methyltransferases (DNMTs) to Epigenetic Marks and Nucleosome Structure Genome-Wide in Human Tumor Cells

ABSTRACT: Linking DNA Methyltransferases (DNMTs) to Epigenetic Marks and Nucleosome Structure Genome-Wide in Human Tumor Cells

PROVIDER: PRJNA169396 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR516143.fastq.gz	Fastqsanger.gz
	SRR516144.fastq.gz	Fastqsanger.gz
	SRR516145.fastq.gz	Fastqsanger.gz
	SRR516146.fastq.gz	Fastqsanger.gz
	SRR516147.fastq.gz	Fastqsanger.gz

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Structure of DNA methyltransferases DNMT3A/DNMT3B bound to a nucleosome [array]

Project description:CpG methylation by the de novo DNA methyltransferases (DNMTs) 3A and 3B is essential for mammalian development and differentiation and is frequently dysregulated in cancer1. These two DNMTs preferentially bind to nucleosomes yet cannot methylate the DNA wrapped around the nucleosome core2, and favor the methylation of linker DNA at positioned nucleosomes3,4. Here we present the cryo-EM structure of a ternary complex of catalytically competent DNMT3A2, the catalytically inactive accessory subunit DNMT3B3, and a nucleosome core particle flanked by linker DNA. The catalytic-like domain of the accessory DNMT3B3 binds the acidic patch of the nucleosome core, which orients the binding of DNMT3A2 to the linker DNA. The steric constraints of this arrangement suggest that nucleosomal DNA must be moved relative to the nucleosome core for de novo methylation to occur. CpG methylation by the de novo DNA methyltransferases (DNMTs) 3A and 3B is essential for mammalian development and differentiation and is frequently dysregulated in cancer1. These two DNMTs preferentially bind to nucleosomes yet cannot methylate the DNA wrapped around the nucleosome core2, and favor the methylation of linker DNA at positioned nucleosomes3,4. Here we present the cryo-EM structure of a ternary complex of catalytically competent DNMT3A2, the catalytically inactive accessory subunit DNMT3B3, and a nucleosome core particle flanked by linker DNA. The catalytic-like domain of the accessory DNMT3B3 binds the acidic patch of the nucleosome core, which orients the binding of DNMT3A2 to the linker DNA. The steric constraints of this arrangement suggest that nucleosomal DNA must be moved relative to the nucleosome core for de novo methylation to occur.

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Linking DNA Methyltransferases (DNMTs) to Epigenetic Marks and Nucleosome Structure Genome-Wide in Human Tumor Cells

Project description:This SuperSeries is composed of the following subset Series: GSE38936: Expression data from human cancer cells GSE38937: Profiling of Chromatin States in a Human Cancer Cell Line Refer to individual Series

2012-10-19 | E-GEOD-38938 | biostudies-arrayexpress

Linking DNA Methyltransferases (DNMTs) to Epigenetic Marks and Nucleosome Structure Genome-Wide in Human Tumor Cells

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

2012-10-19 | GSE38938 | GEO

Nucleosome positioning in Yeast expressing active or inactive murine DNMTs

Project description:Nucleosome positioning in Yeast expressing active or inactive murine DNMTs

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Linking DNA methyltransferases to epigenetic marks and nucleosome structure genome-wide in human tumor cells.

Project description:DNA methylation, mediated by the combined action of three DNA methyltransferases (DNMT1, DNMT3A, and DNMT3B), is essential for mammalian development and is a major contributor to cellular transformation. To elucidate how DNA methylation is targeted, we mapped the genome-wide localization of all DNMTs and methylation, and examined the relationships among these markers, histone modifications, and nucleosome structure in a pluripotent human tumor cell line in its undifferentiated and differentiated states. Our findings reveal a strong link between DNMTs and transcribed loci, and that DNA methylation is not a simple sum of DNMT localization patterns. A comparison of the epigenomes of normal and cancerous stem cells, and pluripotent and differentiated states shows that the presence of at least two DNMTs is strongly associated with loci targeted for DNA hypermethylation. Taken together, these results shed important light on the determinants of DNA methylation and how it may become disrupted in cancer cells.

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DNA methyltransferases are complementary in maintaining DNA methylation in embryonic stem cells

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De novo methylaton of the unmethylated K. phaffii genome by human DNA methyltransferases (DNMTs)

Project description:De novo methylaton of the unmethylated K. phaffii genome by human DNA methyltransferases (DNMTs)

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