The RNA methyltransferase Dnmt2 methylates DNA in the structural context of a tRNA
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Steffen Kaiser
- Tomasz P Jurkowski
- Stefanie Kellner
- Dirk Schneider
- Albert Jeltsch
- Mark Helm
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000417381900015&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1080/15476286.2016.1236170
- eISSN
- 1555-8584
- Externe Identifier
- Clarivate Analytics Document Solution ID: FP1OB
- PubMed Identifier: 27819523
- ISSN
- 1547-6286
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- RNA BIOLOGY
- Schlüsselwörter
- 5-methylcytosine
- DNA
- Dnmt2
- enzyme kinetics
- modification pathway crosstalk
- RNA methylation
- RNA modification
- tRNA
- Paginierung
- 1241 - 1251
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Titel
- The RNA methyltransferase Dnmt2 methylates DNA in the structural context of a tRNA
- Sub types
- Article
- Ausgabe der Zeitschrift
- 14
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Steffen Kaiser
- Tomasz P Jurkowski
- Stefanie Kellner
- Dirk Schneider
- Albert Jeltsch
- Mark Helm
- DOI
- 10.1080/15476286.2016.1236170
- eISSN
- 1555-8584
- ISSN
- 1547-6286
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- RNA Biology
- Sprache
- en
- Online publication date
- 2016
- Paginierung
- 1241 - 1251
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Herausgeber
- Informa UK Limited
- Herausgeber URL
- http://dx.doi.org/10.1080/15476286.2016.1236170
- Datum der Datenerfassung
- 2020
- Titel
- The RNA methyltransferase Dnmt2 methylates DNA in the structural context of a tRNA
- Ausgabe der Zeitschrift
- 14
Datenquelle: Crossref
- Abstract
- The amino acid sequence of Dnmt2 is very similar to the catalytic domains of bacterial and eukaryotic DNA-(cytosine 5)-methyltransferases, but it efficiently catalyzes tRNA methylation, while its DNA methyltransferase activity is the subject of controversial reports with rates varying between zero and very weak. By using composite nucleic acid molecules as substrates, we surprisingly found that DNA fragments, when presented as covalent DNA-RNA hybrids in the structural context of a tRNA, can be more efficiently methylated than the corresponding natural tRNA substrate. Furthermore, by stepwise development of tRNA<sup>Asp</sup>, we showed that this natural Dnmt2 substrate could be engineered to employ RNAs that act like guide RNAs in vitro. The 5'-half of tRNA<sup>Asp</sup> was able to efficiently guide methylation toward a single stranded tRNA fragment as would result from tRNA cleavage by tRNA specific nucleases. In a more artificial setting, a composite system of guide RNAs could ultimately be engineered to enable the enzyme to perform cytidine methylation on single stranded DNA in vitro.
- Addresses
- a Institute of Pharmacy and Biochemistry, Johannes Gutenberg University Mainz , Mainz , Germany.
- Autoren
- Steffen Kaiser
- Tomasz P Jurkowski
- Stefanie Kellner
- Dirk Schneider
- Albert Jeltsch
- Mark Helm
- DOI
- 10.1080/15476286.2016.1236170
- eISSN
- 1555-8584
- Externe Identifier
- PubMed Identifier: 27819523
- PubMed Central ID: PMC5699543
- Open access
- true
- ISSN
- 1547-6286
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- RNA biology
- Schlüsselwörter
- Animals
- Humans
- Mice
- Cytosine
- DNA
- RNA, Transfer
- DNA Methylation
- Nucleic Acid Conformation
- Structure-Activity Relationship
- Methylation
- DNA (Cytosine-5-)-Methyltransferases
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2016
- Open access status
- Open Access
- Paginierung
- 1241 - 1251
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Publisher licence
- CC BY-NC
- Datum der Datenerfassung
- 2016
- Titel
- The RNA methyltransferase Dnmt2 methylates DNA in the structural context of a tRNA.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 14
Files
https://www.tandfonline.com/doi/pdf/10.1080/15476286.2016.1236170?needAccess=true https://europepmc.org/articles/PMC5699543?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- The amino acid sequence of Dnmt2 is very similar to the catalytic domains of bacterial and eukaryotic DNA-(cytosine 5)-methyltransferases, but it efficiently catalyzes tRNA methylation, while its DNA methyltransferase activity is the subject of controversial reports with rates varying between zero and very weak. By using composite nucleic acid molecules as substrates, we surprisingly found that DNA fragments, when presented as covalent DNA-RNA hybrids in the structural context of a tRNA, can be more efficiently methylated than the corresponding natural tRNA substrate. Furthermore, by stepwise development of tRNAAsp, we showed that this natural Dnmt2 substrate could be engineered to employ RNAs that act like guide RNAs in vitro. The 5'-half of tRNAAsp was able to efficiently guide methylation toward a single stranded tRNA fragment as would result from tRNA cleavage by tRNA specific nucleases. In a more artificial setting, a composite system of guide RNAs could ultimately be engineered to enable the enzyme to perform cytidine methylation on single stranded DNA in vitro.
- Autoren
- Steffen Kaiser
- Tomasz P Jurkowski
- Stefanie Kellner
- Dirk Schneider
- Albert Jeltsch
- Mark Helm
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/27819523
- DOI
- 10.1080/15476286.2016.1236170
- eISSN
- 1555-8584
- Externe Identifier
- PubMed Central ID: PMC5699543
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- RNA Biol
- Schlüsselwörter
- 5-methylcytosine
- DNA
- Dnmt2
- RNA methylation
- RNA modification
- enzyme kinetics
- modification pathway crosstalk
- tRNA
- Animals
- Cytosine
- DNA
- DNA (Cytosine-5-)-Methyltransferases
- DNA Methylation
- Humans
- Methylation
- Mice
- Nucleic Acid Conformation
- RNA, Transfer
- Structure-Activity Relationship
- Sprache
- eng
- Country
- United States
- Paginierung
- 1241 - 1251
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2018
- Titel
- The RNA methyltransferase Dnmt2 methylates DNA in the structural context of a tRNA.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 14
Datenquelle: PubMed
- Beziehungen:
- Eigentum von