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  Human TRMT2A methylates tRNA and contributes to translation fidelity

Witzenberger, M., Burczyk, S., Settele, D., Mayer, W., Welp, L. M., Heiss, M., et al. (2023). Human TRMT2A methylates tRNA and contributes to translation fidelity. Nucleic Acids Research, gkad565. doi:10.1093/nar/gkad565.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000D-70A7-8 Version Permalink: https://hdl.handle.net/21.11116/0000-000D-70A8-7
Genre: Journal Article

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 Creators:
Witzenberger, Monika, Author
Burczyk, Sandra, Author
Settele, David, Author
Mayer, Wieland, Author
Welp, Luisa M.1, Author           
Heiss, Matthias, Author
Wagner, Mirko, Author
Monecke, Thomas, Author
Janowski, Robert, Author
Carell, Thomas, Author
Urlaub, Henning1, Author           
Hauck, Stefanie M., Author
Voigt, Aaron, Author
Niessing, Dierk, Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350290              

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 Abstract: 5-Methyluridine (m5U) is one of the most abundant RNA modifications found in cytosolic tRNA. tRNA methyltransferase 2 homolog A (hTRMT2A) is the dedicated mammalian enzyme for m5U formation at tRNA position 54. However, its RNA binding specificity and functional role in the cell are not well understood. Here we dissected structural and sequence requirements for binding and methylation of its RNA targets. Specificity of tRNA modification by hTRMT2A is achieved by a combination of modest binding preference and presence of a uridine in position 54 of tRNAs. Mutational analysis together with cross-linking experiments identified a large hTRMT2A–tRNA binding surface. Furthermore, complementing hTRMT2A interactome studies revealed that hTRMT2A interacts with proteins involved in RNA biogenesis. Finally, we addressed the question of the importance of hTRMT2A function by showing that its knockdown reduces translation fidelity. These findings extend the role of hTRMT2A beyond tRNA modification towards a role in translation.

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Language(s): eng - English
 Dates: 2023-07-03
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1093/nar/gkad565
 Degree: -

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Project name : The Federal Ministry of Education and Research (BMBF) [PolyQure, 16GW0306 and 16GW0307, to A.V. and D.N., respectively]; the Max Planck Society [MPI-NATH.U. to T.C.]; the Bayerische Forschungsstiftung [AZ-1459-20C] to M.H. and M.W.]; the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme [741 912 (EpiR) to M.H. and M.W.]; the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [Project-ID 321812289-GRK 2338 to M.H. and M.W.]; and the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [Project-ID INST 40/656-1 to D.N.]; and the Deutsche Forschungsgemeinschaft (SFB1565) [Project-ID 469281184 to H.U.].
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Funding program : -
Funding organization : -
Project name : EPiR
Grant ID : 741912
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Nucleic Acids Research
  Other : Nucleic Acids Res
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: - Sequence Number: gkad565 Start / End Page: - Identifier: ISSN: 0305-1048
CoNE: https://pure.mpg.de/cone/journals/resource/110992357379342