Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Elisa Vilardo
- Fabian Amman
- Ursula Toth
- Annika Kotter
- Mark Helm
- Walter Rossmanith
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000574284500032&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1093/nar/gkaa353
- eISSN
- 1362-4962
- Externe Identifier
- Clarivate Analytics Document Solution ID: NV4HI
- PubMed Identifier: 32392304
- ISSN
- 0305-1048
- Ausgabe der Veröffentlichung
- 11
- Zeitschrift
- NUCLEIC ACIDS RESEARCH
- Paginierung
- 6157 - 6169
- Datum der Veröffentlichung
- 2020
- Status
- Published
- Titel
- Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B
- Sub types
- Article
- Ausgabe der Zeitschrift
- 48
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Abstract
- <jats:title>Abstract</jats:title> <jats:p>The TRM10 family of methyltransferases is responsible for the N1-methylation of purines at position 9 of tRNAs in Archaea and Eukarya. The human genome encodes three TRM10-type enzymes, of which only the mitochondrial TRMT10C was previously characterized in detail, whereas the functional significance of the two presumably nuclear enzymes TRMT10A and TRMT10B remained unexplained. Here we show that TRMT10A is m1G9-specific and methylates a subset of nuclear-encoded tRNAs, whilst TRMT10B is the first m1A9-specific tRNA methyltransferase found in eukaryotes and is responsible for the modification of a single nuclear-encoded tRNA. Furthermore, we show that the lack of G9 methylation causes a decrease in the steady-state levels of the initiator tRNAiMet-CAT and an alteration in its further post-transcriptional modification. Our work finally clarifies the function of TRMT10A and TRMT10B in vivo and provides evidence that the loss of TRMT10A affects the pool of cytosolic tRNAs required for protein synthesis.</jats:p>
- Autoren
- Elisa Vilardo
- Fabian Amman
- Ursula Toth
- Annika Kotter
- Mark Helm
- Walter Rossmanith
- DOI
- 10.1093/nar/gkaa353
- eISSN
- 1362-4962
- ISSN
- 0305-1048
- Ausgabe der Veröffentlichung
- 11
- Zeitschrift
- Nucleic Acids Research
- Sprache
- en
- Online publication date
- 2020
- Paginierung
- 6157 - 6169
- Datum der Veröffentlichung
- 2020
- Status
- Published
- Herausgeber
- Oxford University Press (OUP)
- Herausgeber URL
- http://dx.doi.org/10.1093/nar/gkaa353
- Datum der Datenerfassung
- 2020
- Titel
- Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B
- Ausgabe der Zeitschrift
- 48
Datenquelle: Crossref
- Abstract
- The TRM10 family of methyltransferases is responsible for the N1-methylation of purines at position 9 of tRNAs in Archaea and Eukarya. The human genome encodes three TRM10-type enzymes, of which only the mitochondrial TRMT10C was previously characterized in detail, whereas the functional significance of the two presumably nuclear enzymes TRMT10A and TRMT10B remained unexplained. Here we show that TRMT10A is m1G9-specific and methylates a subset of nuclear-encoded tRNAs, whilst TRMT10B is the first m1A9-specific tRNA methyltransferase found in eukaryotes and is responsible for the modification of a single nuclear-encoded tRNA. Furthermore, we show that the lack of G9 methylation causes a decrease in the steady-state levels of the initiator tRNAiMet-CAT and an alteration in its further post-transcriptional modification. Our work finally clarifies the function of TRMT10A and TRMT10B in vivo and provides evidence that the loss of TRMT10A affects the pool of cytosolic tRNAs required for protein synthesis.
- Addresses
- Center for Anatomy & Cell Biology, Medical University of Vienna, 1090 Vienna, Austria.
- Autoren
- Elisa Vilardo
- Fabian Amman
- Ursula Toth
- Annika Kotter
- Mark Helm
- Walter Rossmanith
- DOI
- 10.1093/nar/gkaa353
- eISSN
- 1362-4962
- Externe Identifier
- PubMed Identifier: 32392304
- PubMed Central ID: PMC7293042
- Funding acknowledgements
- German Research Foundation: SPP1784
- Austrian Science Fund FWF: P25983
- FWF: F46
- Austrian Science Fund FWF: V 600
- German Research Foundation: MH3397/13-2
- German Research Foundation: MH3397/14-2
- Austrian Science Fund FWF: V600
- Open access
- true
- ISSN
- 0305-1048
- Ausgabe der Veröffentlichung
- 11
- Zeitschrift
- Nucleic acids research
- Schlüsselwörter
- Cell Line
- Humans
- Purines
- Methyltransferases
- tRNA Methyltransferases
- RNA, Transfer
- Protein Biosynthesis
- Base Sequence
- Methylation
- Sprache
- eng
- Medium
- Open access status
- Open Access
- Paginierung
- 6157 - 6169
- Datum der Veröffentlichung
- 2020
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2020
- Titel
- Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 48
Files
https://academic.oup.com/nar/article-pdf/48/11/6157/33384627/gkaa353.pdf https://europepmc.org/articles/PMC7293042?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- The TRM10 family of methyltransferases is responsible for the N1-methylation of purines at position 9 of tRNAs in Archaea and Eukarya. The human genome encodes three TRM10-type enzymes, of which only the mitochondrial TRMT10C was previously characterized in detail, whereas the functional significance of the two presumably nuclear enzymes TRMT10A and TRMT10B remained unexplained. Here we show that TRMT10A is m1G9-specific and methylates a subset of nuclear-encoded tRNAs, whilst TRMT10B is the first m1A9-specific tRNA methyltransferase found in eukaryotes and is responsible for the modification of a single nuclear-encoded tRNA. Furthermore, we show that the lack of G9 methylation causes a decrease in the steady-state levels of the initiator tRNAiMet-CAT and an alteration in its further post-transcriptional modification. Our work finally clarifies the function of TRMT10A and TRMT10B in vivo and provides evidence that the loss of TRMT10A affects the pool of cytosolic tRNAs required for protein synthesis.
- Date of acceptance
- 2020
- Autoren
- Elisa Vilardo
- Fabian Amman
- Ursula Toth
- Annika Kotter
- Mark Helm
- Walter Rossmanith
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/32392304
- DOI
- 10.1093/nar/gkaa353
- eISSN
- 1362-4962
- Externe Identifier
- PubMed Central ID: PMC7293042
- Funding acknowledgements
- Austrian Science Fund FWF: V 600
- Ausgabe der Veröffentlichung
- 11
- Zeitschrift
- Nucleic Acids Res
- Schlüsselwörter
- Base Sequence
- Cell Line
- Humans
- Methylation
- Methyltransferases
- Protein Biosynthesis
- Purines
- RNA, Transfer
- tRNA Methyltransferases
- Sprache
- eng
- Country
- England
- Paginierung
- 6157 - 6169
- PII
- 5835813
- Datum der Veröffentlichung
- 2020
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2020
- Titel
- Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 48
Datenquelle: PubMed
- Beziehungen:
- Eigentum von