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Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA

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  • Sebastian Leidel

    (Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, CH-8093 Zurich, Switzerland)

  • Patrick G. A. Pedrioli

    (Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, CH-8093 Zurich, Switzerland)

  • Tamara Bucher

    (Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, CH-8093 Zurich, Switzerland)

  • Renée Brost

    (University of Toronto, Toronto, Ontario M5S 3E1, Canada)

  • Michael Costanzo

    (University of Toronto, Toronto, Ontario M5S 3E1, Canada)

  • Alexander Schmidt

    (Institute of Molecular Systems Biology, ETH Zurich, Wolfgang-Pauli-Strasse 16, CH-8093 Zurich, Switzerland
    Competence Center for Systems Physiology and Metabolic Diseases, Schafmattstrasse 18, CH-8093 Zurich, Switzerland)

  • Ruedi Aebersold

    (Institute of Molecular Systems Biology, ETH Zurich, Wolfgang-Pauli-Strasse 16, CH-8093 Zurich, Switzerland
    Faculty of Science, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland
    Institute of Systems Biology, 1441 North 34th Street, Seattle, Washington 98103, USA
    Competence Center for Systems Physiology and Metabolic Diseases, Schafmattstrasse 18, CH-8093 Zurich, Switzerland)

  • Charles Boone

    (University of Toronto, Toronto, Ontario M5S 3E1, Canada)

  • Kay Hofmann

    (Bioinformatics Group, Miltenyi Biotec GmbH, Friedrich-Ebert-Strasse 68, 51429 Bergisch-Gladbach, Germany)

  • Matthias Peter

    (Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, CH-8093 Zurich, Switzerland
    Competence Center for Systems Physiology and Metabolic Diseases, Schafmattstrasse 18, CH-8093 Zurich, Switzerland)

Abstract

Evolution of ubiquitin-like systems Covalent attachment of ubiquitin-like proteins (UBLs) can modify a protein's function or localization. In bacteria, UBL homologues act as sulphur carriers. Leidel et al. now show that the oldest UBL protein, Urm1p from yeast, is also a sulphur carrier that modifies transfer RNA. Urm1p is first adenylated by, and then thiolated by, Uba4p, after which the sulphur moiety is transferred to the U34 'wobble' position in cytoplasmic adenylated tRNAs. This finding adds support for the theory that ubiquitin-like systems evolved from bacterial sulphur-carrier systems. The identification of a pathway generating thiolated uridine at the tRNA wobble position might also have therapeutic implications, since HIV reverse transcriptase relies on this modification to initiate reverse transcription of the HIV RNA-genome in vitro.

Suggested Citation

  • Sebastian Leidel & Patrick G. A. Pedrioli & Tamara Bucher & Renée Brost & Michael Costanzo & Alexander Schmidt & Ruedi Aebersold & Charles Boone & Kay Hofmann & Matthias Peter, 2009. "Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA," Nature, Nature, vol. 458(7235), pages 228-232, March.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7235:d:10.1038_nature07643
    DOI: 10.1038/nature07643
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    Cited by:

    1. Sakshi Jain & Lukasz Koziej & Panagiotis Poulis & Igor Kaczmarczyk & Monika Gaik & Michal Rawski & Namit Ranjan & Sebastian Glatt & Marina V. Rodnina, 2023. "Modulation of translational decoding by m6A modification of mRNA," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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