Human DNMT2 methylates tRNAAsp molecules using a DNA methyltransferase-like catalytic mechanism

Publikationstyp:
Zeitschriftenaufsatz
Metadaten:
Autoren
  • Tomasz P Jurkowski
  • Madeleine Meusburger
  • Sameer Phalke
  • Mark Helm
  • Wolfgang Nellen
  • Gunter Reuter
  • Albert Jeltsch
Autoren-URL
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000257800700022&DestLinkType=FullRecord&DestApp=WOS_CPL
DOI
10.1261/rna.970408
eISSN
1469-9001
Externe Identifier
  • Clarivate Analytics Document Solution ID: 328LU
  • PubMed Identifier: 18567810
ISSN
1355-8382
Ausgabe der Veröffentlichung
8
Zeitschrift
RNA
Schlüsselwörter
  • Dnmt2
  • catalytic mechanism
  • RNA methylation
  • tRNAAsp
Paginierung
1663 - 1670
Datum der Veröffentlichung
2008
Status
Published
Titel
Human DNMT2 methylates tRNA<SUP>Asp</SUP> molecules using a DNA methyltransferase-like catalytic mechanism
Sub types
  • Article
Ausgabe der Zeitschrift
14

Datenquelle: Web of Science (Lite)

Andere Metadatenquellen:
Abstract
<jats:p>Although their amino acid sequences and structure closely resemble DNA methyltransferases, Dnmt2 proteins were recently shown by Goll and colleagues to function as RNA methyltransferases transferring a methyl group to the C5 position of C38 in tRNA<jats:sup>Asp</jats:sup>. We observe that human DNMT2 methylates tRNA isolated from Dnmt2 knock-out <jats:italic>Drosophila melanogaster</jats:italic> and <jats:italic>Dictyostelium discoideum</jats:italic>. RNA extracted from wild type <jats:italic>D. melanogaster</jats:italic> was methylated to a lower degree, but in the case of <jats:italic>Dictyostelium</jats:italic>, there was no difference in the methylation of RNA isolated from wild-type and Dnmt2 knock-out strains. Methylation of in vitro transcribed tRNA<jats:sup>Asp</jats:sup> confirms it to be a target of DNMT2. Using site directed mutagenesis, we show here that the enzyme has a DNA methyltransferase-like mechanism, because similar residues from motifs IV, VI, and VIII are involved in catalysis as identified in DNA methyltransferases. In addition, exchange of C292, which is located in a CFT motif conserved among Dnmt2 proteins, strongly reduced the catalytic activity of DNMT2. Dnmt2 represents the first example of an RNA methyltransferase using a DNA methyltransferase type of mechanism.</jats:p>
Autoren
  • Tomasz P Jurkowski
  • Madeleine Meusburger
  • Sameer Phalke
  • Mark Helm
  • Wolfgang Nellen
  • Gunter Reuter
  • Albert Jeltsch
DOI
10.1261/rna.970408
eISSN
1469-9001
ISSN
1355-8382
Ausgabe der Veröffentlichung
8
Zeitschrift
RNA
Sprache
en
Online publication date
2008
Paginierung
1663 - 1670
Datum der Veröffentlichung
2008
Status
Published
Herausgeber
Cold Spring Harbor Laboratory
Herausgeber URL
http://dx.doi.org/10.1261/rna.970408
Datum der Datenerfassung
2021
Titel
Human DNMT2 methylates tRNA<sup>Asp</sup> molecules using a DNA methyltransferase-like catalytic mechanism
Ausgabe der Zeitschrift
14

Datenquelle: Crossref

Abstract
Although their amino acid sequences and structure closely resemble DNA methyltransferases, Dnmt2 proteins were recently shown by Goll and colleagues to function as RNA methyltransferases transferring a methyl group to the C5 position of C38 in tRNA(Asp). We observe that human DNMT2 methylates tRNA isolated from Dnmt2 knock-out Drosophila melanogaster and Dictyostelium discoideum. RNA extracted from wild type D. melanogaster was methylated to a lower degree, but in the case of Dictyostelium, there was no difference in the methylation of RNA isolated from wild-type and Dnmt2 knock-out strains. Methylation of in vitro transcribed tRNA(Asp) confirms it to be a target of DNMT2. Using site directed mutagenesis, we show here that the enzyme has a DNA methyltransferase-like mechanism, because similar residues from motifs IV, VI, and VIII are involved in catalysis as identified in DNA methyltransferases. In addition, exchange of C292, which is located in a CFT motif conserved among Dnmt2 proteins, strongly reduced the catalytic activity of DNMT2. Dnmt2 represents the first example of an RNA methyltransferase using a DNA methyltransferase type of mechanism.
Addresses
  • Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, 28759 Bremen, Germany.
Autoren
  • Tomasz P Jurkowski
  • Madeleine Meusburger
  • Sameer Phalke
  • Mark Helm
  • Wolfgang Nellen
  • Gunter Reuter
  • Albert Jeltsch
DOI
10.1261/rna.970408
eISSN
1469-9001
Externe Identifier
  • PubMed Identifier: 18567810
  • PubMed Central ID: PMC2491481
Open access
false
ISSN
1355-8382
Ausgabe der Veröffentlichung
8
Zeitschrift
RNA (New York, N.Y.)
Schlüsselwörter
  • Animals
  • Humans
  • Drosophila melanogaster
  • Dictyostelium
  • tRNA Methyltransferases
  • RNA, Transfer, Asp
  • Mutagenesis, Site-Directed
  • Sequence Alignment
  • Amino Acid Sequence
  • Molecular Sequence Data
  • DNA (Cytosine-5-)-Methyltransferases
Sprache
eng
Medium
Print-Electronic
Online publication date
2008
Paginierung
1663 - 1670
Datum der Veröffentlichung
2008
Status
Published
Datum der Datenerfassung
2008
Titel
Human DNMT2 methylates tRNA(Asp) molecules using a DNA methyltransferase-like catalytic mechanism.
Sub types
  • Research Support, Non-U.S. Gov't
  • research-article
  • Journal Article
Ausgabe der Zeitschrift
14

Files

http://rnajournal.cshlp.org/content/14/8/1663.full.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18567810/pdf/?tool=EBI http://www.rnajournal.org/cgi/reprint/14/8/1663 https://europepmc.org/articles/PMC2491481?pdf=render

Datenquelle: Europe PubMed Central

Abstract
Although their amino acid sequences and structure closely resemble DNA methyltransferases, Dnmt2 proteins were recently shown by Goll and colleagues to function as RNA methyltransferases transferring a methyl group to the C5 position of C38 in tRNA(Asp). We observe that human DNMT2 methylates tRNA isolated from Dnmt2 knock-out Drosophila melanogaster and Dictyostelium discoideum. RNA extracted from wild type D. melanogaster was methylated to a lower degree, but in the case of Dictyostelium, there was no difference in the methylation of RNA isolated from wild-type and Dnmt2 knock-out strains. Methylation of in vitro transcribed tRNA(Asp) confirms it to be a target of DNMT2. Using site directed mutagenesis, we show here that the enzyme has a DNA methyltransferase-like mechanism, because similar residues from motifs IV, VI, and VIII are involved in catalysis as identified in DNA methyltransferases. In addition, exchange of C292, which is located in a CFT motif conserved among Dnmt2 proteins, strongly reduced the catalytic activity of DNMT2. Dnmt2 represents the first example of an RNA methyltransferase using a DNA methyltransferase type of mechanism.
Autoren
  • Tomasz P Jurkowski
  • Madeleine Meusburger
  • Sameer Phalke
  • Mark Helm
  • Wolfgang Nellen
  • Gunter Reuter
  • Albert Jeltsch
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/18567810
DOI
10.1261/rna.970408
eISSN
1469-9001
Externe Identifier
  • PubMed Central ID: PMC2491481
Ausgabe der Veröffentlichung
8
Zeitschrift
RNA
Schlüsselwörter
  • Amino Acid Sequence
  • Animals
  • DNA (Cytosine-5-)-Methyltransferases
  • Dictyostelium
  • Drosophila melanogaster
  • Humans
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • RNA, Transfer, Asp
  • Sequence Alignment
  • tRNA Methyltransferases
Sprache
eng
Country
United States
Paginierung
1663 - 1670
PII
rna.970408
Datum der Veröffentlichung
2008
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2008
Titel
Human DNMT2 methylates tRNA(Asp) molecules using a DNA methyltransferase-like catalytic mechanism.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
14

Datenquelle: PubMed

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