Literature DB >> 14555475

Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p.

April S Goehring1, David M Rivers, George F Sprague.   

Abstract

Urm1p is a ubiquitin-related protein that serves as a posttranslational modification of other proteins. Urm1p conjugation has been implicated in the budding process and in nutrient sensing. Here, we have identified the first in vivo target for the urmylation pathway as the antioxidant protein Ahp1p. The attachment of Urm1p to Ahp1p requires the E1 for the urmylation pathway, Uba4p. Loss of the urmylation pathway components results in sensitivity to a thiol-specific oxidant, as does loss of Ahp1p, implying that urmylation has a role in an oxidative-stress response. Moreover, treatment of cells with thiol-specific oxidants affects the abundance of Ahp1p-Urm1p conjugates. These results suggest that the conjugation of Urm1p to Ahp1p could regulate the function of Ahp1p in antioxidant stress response in Saccharomyces cerevisiae.

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Year:  2003        PMID: 14555475      PMCID: PMC219378          DOI: 10.1128/EC.2.5.930-936.2003

Source DB:  PubMed          Journal:  Eukaryot Cell        ISSN: 1535-9786


  54 in total

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  56 in total

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Review 7.  Post-translational modification and protein sorting to small extracellular vesicles including exosomes by ubiquitin and UBLs.

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Authors:  Matthew D Petroski; Guy S Salvesen; Dieter A Wolf
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Journal:  Mol Cell Proteomics       Date:  2013-10-04       Impact factor: 5.911

10.  Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA.

Authors:  Sebastian Leidel; Patrick G A Pedrioli; Tamara Bucher; Renée Brost; Michael Costanzo; Alexander Schmidt; Ruedi Aebersold; Charles Boone; Kay Hofmann; Matthias Peter
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