Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Raghuvaran Shanmugam
- Jacob Fierer
- Steffen Kaiser
- Mark Helm
- Tomasz P Jurkowski
- Albert Jeltsch
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000414776800010&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1038/celldisc.2015.10
- eISSN
- 2056-5968
- Externe Identifier
- Clarivate Analytics Document Solution ID: VB1VM
- PubMed Identifier: 27462411
- Zeitschrift
- CELL DISCOVERY
- Schlüsselwörter
- Dnmt2
- tRNA methylation
- aminoacylation
- regulation of translation
- Asp-rich proteins
- Artikelnummer
- ARTN 15011
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Titel
- Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences
- Sub types
- Article
- Ausgabe der Zeitschrift
- 1
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Abstract
- <jats:title>Abstract</jats:title><jats:p>The Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp, but the molecular role of this methylation is unknown. Here, we report that mouse aspartyl-tRNA synthetase shows a four to fivefold preference for C38-methylated tRNA-Asp. Consistently, a 30% reduced charging level of tRNA-Asp was observed in Dnmt2 knockout (KO) murine embryonic fibroblast cells. Gene expression analysis with fluorescent reporter proteins fused to an N-terminal poly-Asp sequence showed that protein synthesis of poly-Asp-tagged reporter proteins was reduced in Dnmt2 KO cells as well. The same effect was observed with endogenous proteins containing poly-Asp sequences, indicating that Dnmt2-mediated C38 methylation of tRNA-Asp regulates the translation of proteins containing poly-Asp sequences. Gene ontology searches for proteins containing poly-Asp sequences in the human proteome showed that a significant number of these proteins have roles in transcriptional regulation and gene expression. Hence, the Dnmt2-mediated methylation of tRNA-Asp exhibits a post-transcriptional regulatory role by controlling the synthesis of a group of target proteins containing poly-Asp sequences.</jats:p>
- Autoren
- Raghuvaran Shanmugam
- Jacob Fierer
- Steffen Kaiser
- Mark Helm
- Tomasz P Jurkowski
- Albert Jeltsch
- DOI
- 10.1038/celldisc.2015.10
- eISSN
- 2056-5968
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- Cell Discovery
- Sprache
- en
- Artikelnummer
- 15010
- Online publication date
- 2015
- Status
- Published online
- Herausgeber
- Springer Science and Business Media LLC
- Herausgeber URL
- http://dx.doi.org/10.1038/celldisc.2015.10
- Datum der Datenerfassung
- 2023
- Titel
- Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences
- Ausgabe der Zeitschrift
- 1
Datenquelle: Crossref
- Abstract
- The Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp, but the molecular role of this methylation is unknown. Here, we report that mouse aspartyl-tRNA synthetase shows a four to fivefold preference for C38-methylated tRNA-Asp. Consistently, a 30% reduced charging level of tRNA-Asp was observed in Dnmt2 knockout (KO) murine embryonic fibroblast cells. Gene expression analysis with fluorescent reporter proteins fused to an N-terminal poly-Asp sequence showed that protein synthesis of poly-Asp-tagged reporter proteins was reduced in Dnmt2 KO cells as well. The same effect was observed with endogenous proteins containing poly-Asp sequences, indicating that Dnmt2-mediated C38 methylation of tRNA-Asp regulates the translation of proteins containing poly-Asp sequences. Gene ontology searches for proteins containing poly-Asp sequences in the human proteome showed that a significant number of these proteins have roles in transcriptional regulation and gene expression. Hence, the Dnmt2-mediated methylation of tRNA-Asp exhibits a post-transcriptional regulatory role by controlling the synthesis of a group of target proteins containing poly-Asp sequences.
- Addresses
- Institute of Biochemistry, Stuttgart University, Faculty of Chemistry , Stuttgart, Germany.
- Autoren
- Raghuvaran Shanmugam
- Jacob Fierer
- Steffen Kaiser
- Mark Helm
- Tomasz P Jurkowski
- Albert Jeltsch
- DOI
- 10.1038/celldisc.2015.10
- eISSN
- 2056-5968
- Externe Identifier
- PubMed Identifier: 27462411
- PubMed Central ID: PMC4860778
- Open access
- true
- ISSN
- 2056-5968
- Zeitschrift
- Cell discovery
- Sprache
- eng
- Medium
- Electronic-eCollection
- Online publication date
- 2015
- Open access status
- Open Access
- Paginierung
- 15010
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2016
- Titel
- Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences.
- Sub types
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 1
Files
https://www.nature.com/articles/celldisc201510.pdf https://europepmc.org/articles/PMC4860778?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- The Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp, but the molecular role of this methylation is unknown. Here, we report that mouse aspartyl-tRNA synthetase shows a four to fivefold preference for C38-methylated tRNA-Asp. Consistently, a 30% reduced charging level of tRNA-Asp was observed in Dnmt2 knockout (KO) murine embryonic fibroblast cells. Gene expression analysis with fluorescent reporter proteins fused to an N-terminal poly-Asp sequence showed that protein synthesis of poly-Asp-tagged reporter proteins was reduced in Dnmt2 KO cells as well. The same effect was observed with endogenous proteins containing poly-Asp sequences, indicating that Dnmt2-mediated C38 methylation of tRNA-Asp regulates the translation of proteins containing poly-Asp sequences. Gene ontology searches for proteins containing poly-Asp sequences in the human proteome showed that a significant number of these proteins have roles in transcriptional regulation and gene expression. Hence, the Dnmt2-mediated methylation of tRNA-Asp exhibits a post-transcriptional regulatory role by controlling the synthesis of a group of target proteins containing poly-Asp sequences.
- Date of acceptance
- 2015
- Autoren
- Raghuvaran Shanmugam
- Jacob Fierer
- Steffen Kaiser
- Mark Helm
- Tomasz P Jurkowski
- Albert Jeltsch
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/27462411
- DOI
- 10.1038/celldisc.2015.10
- Externe Identifier
- PubMed Central ID: PMC4860778
- ISSN
- 2056-5968
- Zeitschrift
- Cell Discov
- Schlüsselwörter
- Asp-rich proteins
- Dnmt2
- aminoacylation
- regulation of translation
- tRNA methylation
- Sprache
- eng
- Country
- England
- Paginierung
- 15010
- PII
- celldisc201510
- Datum der Veröffentlichung
- 2015
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2016
- Titel
- Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 1
Datenquelle: PubMed
- Beziehungen:
- Eigentum von