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Witzenberger, M. ; Burczyk, S.* ; Settele, D. ; Mayer, W.* ; Welp, L.M.* ; Heiss, M.* ; Wagner, M.* ; Monecke, T.* ; Janowski, R. ; Carell, T.* ; Urlaub, H.* ; Hauck, S.M. ; Voigt, A.* ; Niessing, D.

Human TRMT2A methylates tRNA and contributes to translation fidelity.

Nucleic Acids Res. 51, 8691-8710 (2023)
Verlagsversion DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Escherichia-coli; Methyltransferase Trma; Recognition Motifs; Gene; Protein; Architecture; Universal; Precursor; Binding; Enzyme
Sprache englisch
Veröffentlichungsjahr 2023
HGF-Berichtsjahr 2023
ISSN (print) / ISBN 0305-1048
e-ISSN 1362-4962
Zeitschrift Nucleic Acids Research
Quellenangaben Band: 51, Heft: 16, Seiten: 8691-8710 Artikelnummer: , Supplement: ,
Verlag Oxford University Press
Verlagsort Great Clarendon St, Oxford Ox2 6dp, England
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
CF Metabolomics & Proteomics (CF-MPC)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503091-001
G-505700-001
A-630700-001
DOI 10.1093/nar/gkad565
WOS ID 001018198500001
Scopus ID 85170295123
PubMed ID 37395448
Erfassungsdatum 2023-10-18
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