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Eukaryotic Cell, October 2003, p. 930-936, Vol. 2, No. 5
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.5.930-936.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Attachment of the Ubiquitin-Related Protein Urm1p to the Antioxidant Protein Ahp1p

April S. Goehring,{dagger} David M. Rivers, and George F. Sprague Jr.*

Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403-1229

Received 17 July 2003/ Accepted 17 July 2003

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.

* Corresponding author. Mailing address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97303-1229. Phone: (541) 346-5883. Fax: (541) 346-4854. E-mail: gsprague{at}molbio.uoregon.edu.

{dagger} Present address: Howard Hughes Medical Institute, Vollum Institute, Oregon Health and Science University, Portland, OR 97239.

Eukaryotic Cell, October 2003, p. 930-936, Vol. 2, No. 5
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.5.930-936.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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