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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Jüdes A,Ebert F,Bär C,Thüring KL,Harrer A,Klassen R,Helm M,Stark MJ,Schaffrath Rdoi
10.1016/j.febslet.2015.02.024subject
Has Abstractpub_date
2015-04-02 00:00:00pages
904-9issue
8eissn
0014-5793issn
1873-3468pii
S0014-5793(15)00116-7journal_volume
589pub_type
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