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.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

Pedrioli PG,Leidel S,Hofmann K

doi

10.1038/embor.2008.209

subject

Has Abstract

pub_date

2008-12-01 00:00:00

pages

1196-202

issue

12

eissn

1469-221X

issn

1469-3178

pii

embor2008209

journal_volume

9

pub_type

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