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The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase

Author

Listed:
  • Ting-Yu Lin

    (Jagiellonian University)

  • Nour El Hana Abbassi

    (Jagiellonian University
    Postgraduate School of Molecular Medicine)

  • Karol Zakrzewski

    (Jagiellonian University
    Postgraduate School of Molecular Medicine)

  • Andrzej Chramiec-Głąbik

    (Jagiellonian University)

  • Małgorzata Jemioła-Rzemińska

    (Jagiellonian University
    Jagiellonian University)

  • Jan Różycki

    (Jagiellonian University)

  • Sebastian Glatt

    (Jagiellonian University)

Abstract

The Elongator complex catalyzes posttranscriptional tRNA modifications by attaching carboxy-methyl (cm5) moieties to uridine bases located in the wobble position. The catalytic subunit Elp3 is highly conserved and harbors two individual subdomains, a radical S-adenosyl methionine (rSAM) and a lysine acetyltransferase (KAT) domain. The details of its modification reaction cycle and particularly the substrate specificity of its KAT domain remain elusive. Here, we present the co-crystal structure of bacterial Elp3 (DmcElp3) bound to an acetyl-CoA analog and compare it to the structure of a monomeric archaeal Elp3 from Methanocaldococcus infernus (MinElp3). Furthermore, we identify crucial active site residues, confirm the importance of the extended N-terminus for substrate recognition and uncover the specific induction of acetyl-CoA hydrolysis by different tRNA species. In summary, our results establish the clinically relevant Elongator subunit as a non-canonical acetyltransferase and genuine tRNA modification enzyme.

Suggested Citation

  • Ting-Yu Lin & Nour El Hana Abbassi & Karol Zakrzewski & Andrzej Chramiec-Głąbik & Małgorzata Jemioła-Rzemińska & Jan Różycki & Sebastian Glatt, 2019. "The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08579-2
    DOI: 10.1038/s41467-019-08579-2
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    Cited by:

    1. Aviel Even & Giovanni Morelli & Silvia Turchetto & Michal Shilian & Romain Le Bail & Sophie Laguesse & Nathalie Krusy & Ariel Brisker & Alexander Brandis & Shani Inbar & Alain Chariot & Frédéric Saudo, 2021. "ATP-citrate lyase promotes axonal transport across species," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    2. Nour-el-Hana Abbassi & Marcin Jaciuk & David Scherf & Pauline Böhnert & Alexander Rau & Alexander Hammermeister & Michał Rawski & Paulina Indyka & Grzegorz Wazny & Andrzej Chramiec-Głąbik & Dominika D, 2024. "Cryo-EM structures of the human Elongator complex at work," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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