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Mol. Cells 2013; 35(3): 210-218

Published online March 31, 2013

https://doi.org/10.1007/s10059-013-2258-0

© The Korean Society for Molecular and Cellular Biology

Saccharomyces cerevisiae KNU5377 Stress Response during High-Temperature Ethanol Fermentation

Il-Sup Kim, Young-Saeng Kim, Hyun Kim, Ingnyol Jin, and Ho-Sung Yoon

Advanced Bio-resource Research Center, 2Department of Biology, 3Department of Microbiology, Kyungpook National University, Daegu 702-701, Korea

Received: October 8, 2012; Revised: November 7, 2012; Accepted: November 8, 2012

Abstract

Fuel ethanol production is far more costly to produce than
fossil fuels. There are a number of approaches to costeffective
fuel ethanol production from biomass. We characterized stress response of thermotolerant Saccharomyces cerevisiae KNU5377 during glucose-based batch fermentation at high temperature (40°C). S. cerevisiae KNU5377 (KNU5377) transcription factors (Hsf1, Msn2/4, and Yap1), metabolic enzymes (hexokinase, glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase, and alcohol dehydrogenase), antioxidant enzymes (thioredoxin 3, thioredoxin reductase, and porin), and molecular chaperones and its cofactors (Hsp104, Hsp82, Hsp60, Hsp42, Hsp30, Hsp26, Cpr1, Sti1, and Zpr1) are upregulated during fermentation, in comparison to S. cerevisiae S288C (S288C). Expression of glyceraldehyde-3-phosphate dehydrogenase increased significantly in KNU5377 cells. In addition, cellular hydroperoxide and protein oxidation, particularly lipid peroxidation of triosephosphate isomerase, was lower in KNU5377 than in S288C. Thus, KNU5377 activates various cell rescue proteins through transcription activators, improving tolerance and increasing alcohol yield by rapidly responding to fermentation stress through redox homeostasis and proteostasis.

Keywords cell rescue protein, high-temperature fermentation, redox state, Saccharomyces cerevisiae KNU5377, stress response

Article

Research Article

Mol. Cells 2013; 35(3): 210-218

Published online March 31, 2013 https://doi.org/10.1007/s10059-013-2258-0

Copyright © The Korean Society for Molecular and Cellular Biology.

Saccharomyces cerevisiae KNU5377 Stress Response during High-Temperature Ethanol Fermentation

Il-Sup Kim, Young-Saeng Kim, Hyun Kim, Ingnyol Jin, and Ho-Sung Yoon

Advanced Bio-resource Research Center, 2Department of Biology, 3Department of Microbiology, Kyungpook National University, Daegu 702-701, Korea

Received: October 8, 2012; Revised: November 7, 2012; Accepted: November 8, 2012

Abstract

Fuel ethanol production is far more costly to produce than
fossil fuels. There are a number of approaches to costeffective
fuel ethanol production from biomass. We characterized stress response of thermotolerant Saccharomyces cerevisiae KNU5377 during glucose-based batch fermentation at high temperature (40°C). S. cerevisiae KNU5377 (KNU5377) transcription factors (Hsf1, Msn2/4, and Yap1), metabolic enzymes (hexokinase, glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase, and alcohol dehydrogenase), antioxidant enzymes (thioredoxin 3, thioredoxin reductase, and porin), and molecular chaperones and its cofactors (Hsp104, Hsp82, Hsp60, Hsp42, Hsp30, Hsp26, Cpr1, Sti1, and Zpr1) are upregulated during fermentation, in comparison to S. cerevisiae S288C (S288C). Expression of glyceraldehyde-3-phosphate dehydrogenase increased significantly in KNU5377 cells. In addition, cellular hydroperoxide and protein oxidation, particularly lipid peroxidation of triosephosphate isomerase, was lower in KNU5377 than in S288C. Thus, KNU5377 activates various cell rescue proteins through transcription activators, improving tolerance and increasing alcohol yield by rapidly responding to fermentation stress through redox homeostasis and proteostasis.

Keywords: cell rescue protein, high-temperature fermentation, redox state, Saccharomyces cerevisiae KNU5377, stress response

Mol. Cells
May 31, 2022 Vol.45 No.5, pp. 273~352
COVER PICTURE
Fe2+ ion depletion-induced expression of BΔGFP at the early stage of leaf development (Choi et al., pp. 294-305).

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