Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation
- Publication type:
- Journal article
- Metadata:
-
- Autoren
- Albert Jeltsch
- Ann Ehrenhofer-Murray
- Tomasz P Jurkowski
- Frank Lyko
- Gunter Reuterd
- Serge Ankri
- Wolfgang Nellen
- Matthias Schaefer
- Mark Helm
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000417381900004&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1080/15476286.2016.1191737
- eISSN
- 1555-8584
- Externe Identifier
- Clarivate Analytics Document Solution ID: FP1OB
- PubMed Identifier: 27232191
- ISSN
- 1547-6286
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- RNA BIOLOGY
- Schlüsselwörter
- DNA methylation
- epigenetics
- methylcytidine
- RNA methylation
- tRNA
- Paginierung
- 1108 - 1123
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Titel
- Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation
- Sub types
- Review
- Ausgabe der Zeitschrift
- 14
Data source: Web of Science (Lite)
- Other metadata sources:
-
- Autoren
- Albert Jeltsch
- Ann Ehrenhofer-Murray
- Tomasz P Jurkowski
- Frank Lyko
- Gunter Reuter
- Serge Ankri
- Wolfgang Nellen
- Matthias Schaefer
- Mark Helm
- DOI
- 10.1080/15476286.2016.1191737
- eISSN
- 1555-8584
- ISSN
- 1547-6286
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- RNA Biology
- Sprache
- en
- Online publication date
- 2016
- Paginierung
- 1108 - 1123
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Herausgeber
- Informa UK Limited
- Herausgeber URL
- http://dx.doi.org/10.1080/15476286.2016.1191737
- Datum der Datenerfassung
- 2022
- Titel
- Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation
- Ausgabe der Zeitschrift
- 14
Data source: Crossref
- Abstract
- A group of homologous nucleic acid modification enzymes called Dnmt2, Trdmt1, Pmt1, DnmA, and Ehmet in different model organisms catalyze the transfer of a methyl group from the cofactor S-adenosyl-methionine (SAM) to the carbon-5 of cytosine residues. Originally considered as DNA MTases, these enzymes were shown to be tRNA methyltransferases about a decade ago. Between the presumed involvement in DNA modification-related epigenetics, and the recent foray into the RNA modification field, significant progress has characterized Dnmt2-related research. Here, we review this progress in its diverse facets including molecular evolution, structural biology, biochemistry, chemical biology, cell biology and epigenetics.
- Addresses
- a Institute of Biochemistry , Stuttgart University , Stuttgart , Germany.
- Autoren
- Albert Jeltsch
- Ann Ehrenhofer-Murray
- Tomasz P Jurkowski
- Frank Lyko
- Gunter Reuter
- Serge Ankri
- Wolfgang Nellen
- Matthias Schaefer
- Mark Helm
- DOI
- 10.1080/15476286.2016.1191737
- eISSN
- 1555-8584
- Externe Identifier
- PubMed Identifier: 27232191
- PubMed Central ID: PMC5699548
- Open access
- true
- ISSN
- 1547-6286
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- RNA biology
- Schlüsselwörter
- Animals
- Humans
- Cell Transformation, Neoplastic
- Nucleic Acids
- Retroelements
- Phylogeny
- DNA Methylation
- Gene Expression Regulation
- Epigenesis, Genetic
- Gene Silencing
- Binding Sites
- Protein Binding
- Structure-Activity Relationship
- Substrate Specificity
- Methylation
- Catalysis
- DNA (Cytosine-5-)-Methyltransferases
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2016
- Open access status
- Open Access
- Paginierung
- 1108 - 1123
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Publisher licence
- CC BY-NC
- Datum der Datenerfassung
- 2016
- Titel
- Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation.
- Sub types
- Research Support, Non-U.S. Gov't
- review-article
- Review
- Journal Article
- Ausgabe der Zeitschrift
- 14
Files
https://www.tandfonline.com/doi/pdf/10.1080/15476286.2016.1191737?needAccess=true https://europepmc.org/articles/PMC5699548?pdf=render
Data source: Europe PubMed Central
- Abstract
- A group of homologous nucleic acid modification enzymes called Dnmt2, Trdmt1, Pmt1, DnmA, and Ehmet in different model organisms catalyze the transfer of a methyl group from the cofactor S-adenosyl-methionine (SAM) to the carbon-5 of cytosine residues. Originally considered as DNA MTases, these enzymes were shown to be tRNA methyltransferases about a decade ago. Between the presumed involvement in DNA modification-related epigenetics, and the recent foray into the RNA modification field, significant progress has characterized Dnmt2-related research. Here, we review this progress in its diverse facets including molecular evolution, structural biology, biochemistry, chemical biology, cell biology and epigenetics.
- Autoren
- Albert Jeltsch
- Ann Ehrenhofer-Murray
- Tomasz P Jurkowski
- Frank Lyko
- Gunter Reuter
- Serge Ankri
- Wolfgang Nellen
- Matthias Schaefer
- Mark Helm
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/27232191
- DOI
- 10.1080/15476286.2016.1191737
- eISSN
- 1555-8584
- Externe Identifier
- PubMed Central ID: PMC5699548
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- RNA Biol
- Schlüsselwörter
- DNA methylation
- RNA methylation
- epigenetics
- methylcytidine
- tRNA
- Animals
- Binding Sites
- Catalysis
- Cell Transformation, Neoplastic
- DNA (Cytosine-5-)-Methyltransferases
- DNA Methylation
- Epigenesis, Genetic
- Gene Expression Regulation
- Gene Silencing
- Humans
- Methylation
- Nucleic Acids
- Phylogeny
- Protein Binding
- Retroelements
- Structure-Activity Relationship
- Substrate Specificity
- Sprache
- eng
- Country
- United States
- Paginierung
- 1108 - 1123
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2018
- Titel
- Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation.
- Sub types
- Journal Article
- Review
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 14
Data source: PubMed
- Beziehungen:
- Property of