Adaptive stress response to menadione-induced oxidative stress in Saccharomyces cerevisiae KNU5377

2011 ◽  
Vol 49 (5) ◽  
pp. 816-823 ◽  
Author(s):  
Il-Sup Kim ◽  
Ho-Yong Sohn ◽  
Ingnyol Jin
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Stress Response ◽  
Adaptive Stress Response ◽  
Saccharomyces Cerevisiae Knu5377

scholarly journals Saccharomyces cerevisiae KNU5377 stress response during high-temperature ethanol fermentation

2013 ◽  
Vol 35 (3) ◽  
pp. 210-218 ◽  
Author(s):  
Il-Sup Kim ◽  
Young-Saeng Kim ◽  
Hyun Kim ◽  
Ingnyol Jin ◽  
Ho-Sung Yoon
Keyword(s):  
Saccharomyces Cerevisiae ◽  
High Temperature ◽  
Stress Response ◽  
Ethanol Fermentation ◽  
Saccharomyces Cerevisiae Knu5377

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.

scholarly journals Role of Heat Shock Transcription Factor in Saccharomyces cerevisiae Oxidative Stress Response

2007 ◽  
Vol 6 (8) ◽  
pp. 1373-1379 ◽  
Author(s):  
Ayako Yamamoto ◽  
Junko Ueda ◽  
Noritaka Yamamoto ◽  
Naoya Hashikawa ◽  
Hiroshi Sakurai
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Transcription Factor ◽  
Stress Response ◽  
Heat Shock ◽  
Superoxide Anion ◽  
Target Genes ◽  
Oxidative Stress Response ◽  
Heat Shock Transcription Factor ◽  
Negative Regulator

ABSTRACT The heat shock transcription factor Hsf1 of the yeast Saccharomyces cerevisiae regulates the transcription of a set of genes that contain heat shock elements (HSEs) in their promoters and function in diverse cellular processes, including protein folding. Here, we show that Hsf1 activates the transcription of various target genes when cells are treated with oxidizing reagents, including the superoxide anion generators menadione and KO2 and the thiol oxidants diamide and 1-chloro-2,4-dinitrobenzene (CDNB). Similar to heat shock, the oxidizing reagents are potent inducers of both efficient HSE binding and extensive phosphorylation of Hsf1. The inducible phosphorylation of Hsf1 is regulated by the intramolecular domain-domain interactions and affects HSE structure-specific transcription. Unlike the heat shock, diamide, or CDNB response, menadione or KO2 activation of Hsf1 is inhibited by cyclic-AMP-dependent protein kinase (PKA) activity, which negatively regulates the activator functions of other transcriptional regulators implicated in the oxidative stress response. These results demonstrate that Hsf1 is a member of the oxidative stress-responsive activators and that PKA is a general negative regulator in the superoxide anion response.

Sign in / Sign up

Export Citation Format

Share Document