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Urmylation and tRNA thiolation functions of ubiquitin‐like Uba4·Urm1 systems are conserved from yeast to man
Author(s) -
Jüdes André,
Ebert Folke,
Bär Christian,
Thüring Kathrin L.,
Harrer Aileen,
Klassen Roland,
Helm Mark,
Stark Michael J.R.,
Schaffrath Raffael
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.02.024
Subject(s) - yeast , ubiquitin , saccharomyces cerevisiae , biology , transfer rna , peroxiredoxin , activator (genetics) , biochemistry , budding yeast , function (biology) , gene , conserved sequence , genetics , microbiology and biotechnology , rna , enzyme , peptide sequence , peroxidase
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.