Abstract:
:The ubiquitin-like protein Urm1 can be covalently conjugated to other proteins, such as the yeast thioredoxin peroxidase protein Ahp1p, through a mechanism involving the ubiquitin E1-like enzyme Uba4. Recent findings have revealed a second function of Urm1 as a sulphur carrier in the thiolation of eukaryotic cytoplasmic transfer RNAs (tRNAs). Interestingly, this new role of Urm1 is similar to the sulphur-carrier activity of its prokaryotic counterparts, strengthening the hypothesis that Urm1 is a molecular fossil of the ubiquitin-like protein family. Here, we discuss the function of Urm1 in light of its dual role in protein and RNA modification.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Pedrioli PG,Leidel S,Hofmann Kdoi
10.1038/embor.2008.209subject
Has Abstractpub_date
2008-12-01 00:00:00pages
1196-202issue
12eissn
1469-221Xissn
1469-3178pii
embor2008209journal_volume
9pub_type
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