Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man

André Jüdes, Folke Ebert, Christian Bär, Kathrin L. Thüring, Aileen Harrer, Roland Klassen, Mark Helm, Michael J. R. Stark, Raffael Schaffrath (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    18 Citations (Scopus)

    Abstract

    The ubiquitin-like protein Urm1 from budding yeast and its E1-like activator Uba4 have dual roles in protein urmylation and tRNA thiolation pathways. To study whether these are conserved among eukaryotes, we used gene shuffles to replace the yeast proteins by their human counterparts, hURM1 and hUBA4/MOCS3. As judged from biochemical and genetical assays, hURM1 and hUBA4 are functional in yeast, albeit at reduced efficiencies. They mediate urmylation of the peroxiredoxin Ahp1, a known urmylation target in yeast, and support tRNA thiolation. Similar to hUBA4, yeast Uba4 itself is modified by Urm1 and hURM1 suggesting target overlap between eukaryal urmylation pathways. In sum, our study shows that dual-function ubiquitin-like Urm1·Uba4 systems are conserved and exchangeable between human and yeast cells.

    Original languageEnglish
    Pages (from-to)904-909
    Number of pages6
    JournalFEBS Letters
    Volume589
    Issue number8
    Early online date3 Mar 2015
    DOIs
    Publication statusPublished - 2 Apr 2015

    Keywords

    • Saccharomyces cerevisiae
    • tRNA thiolation
    • Uba4 (hUBA4/MOCS3)
    • Ubiquitin-like urmylation
    • Urm1 (hURM1)

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