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Human TRMT2A methylates tRNA and contributes to translation fidelity.
Nucleic Acids Res. 51, 8691-8710 (2023)
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
ISSN (print) / ISBN
0305-1048
e-ISSN
1362-4962
Zeitschrift
Nucleic Acids Research
Quellenangaben
Band: 51,
Heft: 16,
Seiten: 8691-8710
Verlag
Oxford University Press
Verlagsort
Great Clarendon St, Oxford Ox2 6dp, England
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed