scholarly journals HSF1-mediated oxidative stress response to menadione in <i>Saccharomyces cerevisiae</i> KNU5377Y3 by using proteomic approach

2013 ◽  
Vol 04 (01) ◽  
pp. 44-54 ◽  
Author(s):  
Il-Sup Kim ◽  
Hyun Kim ◽  
Young-Saeng Kim ◽  
Ingnyol Jin ◽  
Ho-Sung Yoon
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Stress Response ◽  
Oxidative Stress Response ◽  
Proteomic Approach

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

2003 ◽  
Vol 2 (5) ◽  
pp. 930-936 ◽  
Author(s):  
April S. Goehring ◽  
David M. Rivers ◽  
George F. Sprague
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Stress Response ◽  
Posttranslational Modification ◽  
Oxidative Stress Response ◽  
Nutrient Sensing ◽  
Related Protein ◽  
Antioxidant Protein ◽  
Antioxidant Stress

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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