Expression of murine DNA methyltransferases Dnmt1 and Dnmt3a in the yeast <i>Saccharomyces cerevisiae</i>

Bulkowska, Urszula; Ishikawa, Takao; Kurlandzka, Anna; Trzcińska-Danielewicz, Joanna; Derlacz, Rafał; Fronk, Jan

doi:10.1002/yea.1538

Cited by 12 publications

(9 citation statements)

References 58 publications

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“…Introduction of the murine methyltransferases Dnmt1 or Dnmt3a leads to detectable, but extremely low levels of DNA methylation (Bulkowska et al 2007). In contrast, a substantially higher level of de novo methylation can be achieved in yeast by coexpressing murine Dnmt3a and Dnmt3L (Hu et al 2009).…”

Section: Interplay Between Dna Methylation and Histone Modificationmentioning

confidence: 99%

Structural and Functional Coordination of DNA and Histone Methylation

Cheng

2014

Cold Spring Harbor Perspectives in Biology

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SUMMARY One of the most fundamental questions in the control of gene expression in mammals is how epigenetic methylation patterns of DNA and histones are established, erased, and recognized. This central process in controlling gene expression includes coordinated covalent modifications of DNA and its associated histones. This article focuses on structural aspects of enzymatic activities of histone (arginine and lysine) methylation and demethylation and functional links between the methylation status of the DNA and histones. An interconnected network of methyltransferases, demethylases, and accessory proteins is responsible for changing or maintaining the modification status of specific regions of chromatin.

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Section: Interplay Between Dna Methylation and Histone Modificationmentioning

confidence: 99%

Structural and Functional Coordination of DNA and Histone Methylation

Cheng

2014

Cold Spring Harbor Perspectives in Biology

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“…Introduction of the murine methyltransferase Dnmt1 or -3a in yeast leads to detectable, but extremely low levels of DNA methylation [34]. By contrast, a substantially higher level of de novo methylation could be achieved in yeast by coexpressing murine Dnmt3a and -3L [32].…”

Section: Add Domains Of Dnmt3l/3a/3b Link Dna Methylation To Unmethylmentioning

confidence: 99%

Molecular Coupling of DNA Methylation and Histone Methylation

2010

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The combinatorial pattern of DNA and histone modifications constitutes an epigenetic ‘code’ that shapes gene-expression patterns by enabling or restricting the transcriptional potential of genomic domains. DNA methylation is associated with histone modifications, particularly the absence of histone H3 lysine 4 methylation (H3K4me0) and the presence of H3K9 methylation. This article focuses on three protein domains (ATRX–Dnmt3–Dnmt3L [ADD], Cys–X–X–Cys [CXXC] and the methyl-CpG-binding domain [MBD]) and the functional implications of domain architecture in the mechanisms linking histone methylation and DNA methylation in mammalian cells. The DNA methyltransferase DNMT3a and its accessory protein DNMT3L contain a H3K4me0-interacting ADD domain that links the DNA methylation reaction with unmodified H3K4. The H3K4 methyltransferase MLL1 contains a CpG-interacting CXXC domain that may couple the H3K4 methylation reaction to unmethylated DNA. Another H3K4 methyltransferase, SET1, although lacking an intrinsic CXXC domain, interacts directly with an accessory protein CFP1 that contains the same domain. The H3K9 methyltransferase SETDB1 contains a putative MBD that potentially links the H3K4 methylation reaction to methylated DNA or may do so through the interaction with the MBD containing protein MBD1. Finally, we consider the domain structure of the DNA methyltransferase DNMT1, its accessory protein UHRF1 and their associated proteins, and propose a mechanism by which DNA methylation and histone methylation may be coordinately maintained through mitotic cell division, allowing for the transmission of parental DNA and for the histone methylation patterns to be copied to newly replicated chromatin.

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“…Introducing the murine maintenance methyltransferase Dnmt1, or Dnmt3a alone, leads to detectable but extremely low levels of DNA methylation in yeast (110). Through joint expression of murine Dnmt3a and Dnmt3L, Hu et al (111) achieved substantially higher levels of de novo methylation.…”

Section: Linking Dna Methylation To H3k4 and H3k9 Methylationmentioning

confidence: 99%

Coordinated Chromatin Control: Structural and Functional Linkage of DNA and Histone Methylation

2010

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One of the most fundamental questions in the control of gene expression in mammals is how epigenetic methylation patterns of DNA and histones are established, erased, and recognized. This central process in controlling metazoan gene expression includes coordinated covalent modifications of DNA and its associated histones. This review focuses on recent developments in characterizing the functional links between the methylation status of the DNA and of two particularly important histone marks. Mammalian DNA methylation is intricately connected to the presence of unmodified lysine 4 and methylated lysine 9 residues in histone H3. An interconnected network of methyltransferases, demethylases, and accessory proteins is responsible for changing or maintaining the modification status of specific regions of chromatin. The structural and functional interactions among members of this network are critical to processes that include imprinting and differentiation, dysregulation of which is associated with disorders ranging from inflammation to cancer.

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Expression of murine DNA methyltransferases Dnmt1 and Dnmt3a in the yeast Saccharomyces cerevisiae

Cited by 12 publications

References 58 publications

Structural and Functional Coordination of DNA and Histone Methylation

Structural and Functional Coordination of DNA and Histone Methylation

Molecular Coupling of DNA Methylation and Histone Methylation

Coordinated Chromatin Control: Structural and Functional Linkage of DNA and Histone Methylation

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