Urm1 at the crossroad of modifications. 'Protein Modifications: Beyond the Usual Suspects' Review Series.
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.
Pedrioli
Patrick G A
PG
Institute of Biochemistry, ETH Zürich, Schafmattstrasse 18, CH-8093 Zürich, Switzerland.
Leidel
Sebastian
S
Hofmann
Kay
K
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D010641:Phenotype; D011499:Protein Processing, Post-Translational; D013455:Sulfur / Q000378:metabolism; D014452:Ubiquitins / Q000737:chemistry / Q000378:metabolism*
D002352:Carrier Proteins; D014452:Ubiquitins; D013455:Sulfur