Editorial-Role of DNA Methyltransferases in the Epigenome.

DNA Methylation DNA methyltransferase function DNA methyltransferase mechanism DNA methyltransferase regulation DNA methyltransferase structure DNMT1 DNMT3A DNMT3B

Journal

Genes
ISSN: 2073-4425
Titre abrégé: Genes (Basel)
Pays: Switzerland
ID NLM: 101551097

Informations de publication

Date de publication:
30 07 2019
Historique:
received: 18 07 2019
accepted: 25 07 2019
entrez: 2 8 2019
pubmed: 2 8 2019
medline: 10 1 2020
Statut: epublish

Résumé

DNA methylation, a modification found in most species, regulates chromatin functions in conjunction with other epigenome modifications, such as histone post-translational modifications and non-coding RNAs. In mammals, DNA methylation has essential roles in development by orchestrating the generation and maintenance of the phenotypic diversity of human cell types. This Special Issue of Genes contains eight review articles, which cover several aspects of epigenome regulation by DNA methyltransferases (DNMTs), the enzymes responsible for the introduction of DNA methylation. The manuscripts present the most recent advances regarding the structure and function of DNMTs, their targeting and regulation by interacting factors and chromatin modifications, and the roles of DNMTs in mammalian development and human diseases. However, many aspects of these important enzymes are still insufficiently understood. Potential directions of future work are the regulation of DNMTs by post-translational modifications and their connection to cellular signaling and second messenger cascades on one hand and to large multifactorial epigenetic chromatin circuits on the other. Additionally, technical advancements, including the availability of designer nucleosomes and the rapid development of cryo-electron microscopy are expected to trigger breakthrough discoveries in this exciting field.

Identifiants

pubmed: 31366147
pii: genes10080574
doi: 10.3390/genes10080574
pmc: PMC6723798
pii:
doi:

Substances chimiques

DNA (Cytosine-5-)-Methyltransferases EC 2.1.1.37

Types de publication

Editorial Introductory Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NCI NIH HHS
ID : P30 CA016672
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM118654
Pays : United States

Déclaration de conflit d'intérêts

The authors declare no conflicts of interest.

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Auteurs

Albert Jeltsch (A)

Department of Biochemistry, Institute of Biochemistry and Technical Biochemistry, University of Stuttgart, 70569 Stuttgart, Germany. albert.jeltsch@ibtb.uni-stuttgart.de.

Humaira Gowher (H)

Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA. hgowher@purdue.edu.

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Classifications MeSH