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Biogenesis and functions of aminocarboxypropyluridine in tRNA

Author

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  • Mayuko Takakura

    (The University of Tokyo)

  • Kensuke Ishiguro

    (The University of Tokyo)

  • Shinichiro Akichika

    (The University of Tokyo)

  • Kenjyo Miyauchi

    (The University of Tokyo)

  • Tsutomu Suzuki

    (The University of Tokyo)

Abstract

Transfer (t)RNAs contain a wide variety of post-transcriptional modifications, which play critical roles in tRNA stability and functions. 3-(3-amino-3-carboxypropyl)uridine (acp3U) is a highly conserved modification found in variable- and D-loops of tRNAs. Biogenesis and functions of acp3U have not been extensively investigated. Using a reverse-genetic approach supported by comparative genomics, we find here that the Escherichia coli yfiP gene, which we rename tapT (tRNA aminocarboxypropyltransferase), is responsible for acp3U formation in tRNA. Recombinant TapT synthesizes acp3U at position 47 of tRNAs in the presence of S-adenosylmethionine. Biochemical experiments reveal that acp3U47 confers thermal stability on tRNA. Curiously, the ΔtapT strain exhibits genome instability under continuous heat stress. We also find that the human homologs of tapT, DTWD1 and DTWD2, are responsible for acp3U formation at positions 20 and 20a of tRNAs, respectively. Double knockout cells of DTWD1 and DTWD2 exhibit growth retardation, indicating that acp3U is physiologically important in mammals.

Suggested Citation

  • Mayuko Takakura & Kensuke Ishiguro & Shinichiro Akichika & Kenjyo Miyauchi & Tsutomu Suzuki, 2019. "Biogenesis and functions of aminocarboxypropyluridine in tRNA," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13525-3
    DOI: 10.1038/s41467-019-13525-3
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    Cited by:

    1. Gabrielle Bourgeois & Pierre-Damien Coureux & Christine Lazennec-Schurdevin & Clément Madru & Thomas Gaillard & Magalie Duchateau & Julia Chamot-Rooke & Sophie Bourcier & Yves Mechulam & Emmanuelle Sc, 2025. "Structures of Saccharolobus solfataricus initiation complexes with leaderless mRNAs highlight archaeal features and eukaryotic proximity," Nature Communications, Nature, vol. 16(1), pages 1-18, December.

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