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



Publication Details
Authors:
Jüdes, A.; Ebert, F.; Bär, C.; Thüring, K.; Harrer, A.; Klassen, R.; Helm, M.; Stark, M.; Schaffrath, R.
Publication year:
2015
Journal:
FEBS Letters
Pages range:
904-909
Volume number:
589
Issue number:
8
Start page:
904
End page:
909
ISSN:
0014-5793

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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.


Keywords
Saccharomyces cerevisiae, Uba4 (hUBA4/MOCS3), Ubiquitin-like urmylation, Urm1 (hURM1)


Authors/Editors

Last updated on 2019-25-07 at 19:12