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Urm1 at the crossroad of modifications. 'Protein Modifications: Beyond the Usual Suspects' Review Series.

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.

SUBMITTER: Pedrioli PG

PROVIDER: S-EPMC2603462 | biostudies-other | 2008 Dec

REPOSITORIES: biostudies-other

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