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Heat shock causes oxidative stress and induces a variety of cell rescue proteins in Saccharomyces cerevisiae KNU5377.
J Microbiol. 2006 Oct; 44(5):492-501.JM

Abstract

In this study, we attempted to characterize the physiological response to oxidative stress by heat shock in Saccharomyces cerevisiae KNU5377 (KNU5377) that ferments at a temperature of 40 degrees C. The KNU5377 strain evidenced a very similar growth rate at 40 degrees C as was recorded under normal conditions. Unlike the laboratory strains of S. cerevisiae, the cell viability of KNU5377 was affected slightly under 2 hours of heat stress conditions at 43 degrees C. KNU5377 evidenced a time-dependent increase in hydroperoxide levels, carbonyl contents, and malondialdehyde (MDA), which increased in the expression of a variety of cell rescue proteins containing Hsp104p, Ssap, Hsp30p, Sod1p, catalase, glutathione reductase, G6PDH, thioredoxin, thioredoxin peroxidase (Tsa1p), Adhp, Aldp, trehalose and glycogen at high temperature. Pma1/2p, Hsp90p and H+-ATPase expression levels were reduced as the result of exposure to heat shock. With regard to cellular fatty acid composition, levels of unsaturated fatty acids (USFAs) were increased significantly at high temperatures (43 degrees C), and this was particularly true of oleic acid (C18:1). The results of this study indicated that oxidative stress as the result of heat shock may induce a more profound stimulation of trehalose, antioxidant enzymes, and heat shock proteins, as well as an increase in the USFAs ratios. This might contribute to cellular protective functions for the maintenance of cellular homeostasis, and may also contribute to membrane fluidity.

Authors+Show Affiliations

Department of Microbiology, Kyungpook National University, Daegu 702-701, Republic of Korea.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17082742

Citation

Kim, Il-Sup, et al. "Heat Shock Causes Oxidative Stress and Induces a Variety of Cell Rescue Proteins in Saccharomyces Cerevisiae KNU5377." Journal of Microbiology (Seoul, Korea), vol. 44, no. 5, 2006, pp. 492-501.
Kim IS, Moon HY, Yun HS, et al. Heat shock causes oxidative stress and induces a variety of cell rescue proteins in Saccharomyces cerevisiae KNU5377. J Microbiol. 2006;44(5):492-501.
Kim, I. S., Moon, H. Y., Yun, H. S., & Jin, I. (2006). Heat shock causes oxidative stress and induces a variety of cell rescue proteins in Saccharomyces cerevisiae KNU5377. Journal of Microbiology (Seoul, Korea), 44(5), 492-501.
Kim IS, et al. Heat Shock Causes Oxidative Stress and Induces a Variety of Cell Rescue Proteins in Saccharomyces Cerevisiae KNU5377. J Microbiol. 2006;44(5):492-501. PubMed PMID: 17082742.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Heat shock causes oxidative stress and induces a variety of cell rescue proteins in Saccharomyces cerevisiae KNU5377. AU - Kim,Il-Sup, AU - Moon,Hye-Youn, AU - Yun,Hae-Sun, AU - Jin,Ingnyol, PY - 2006/11/4/pubmed PY - 2007/2/27/medline PY - 2006/11/4/entrez SP - 492 EP - 501 JF - Journal of microbiology (Seoul, Korea) JO - J Microbiol VL - 44 IS - 5 N2 - In this study, we attempted to characterize the physiological response to oxidative stress by heat shock in Saccharomyces cerevisiae KNU5377 (KNU5377) that ferments at a temperature of 40 degrees C. The KNU5377 strain evidenced a very similar growth rate at 40 degrees C as was recorded under normal conditions. Unlike the laboratory strains of S. cerevisiae, the cell viability of KNU5377 was affected slightly under 2 hours of heat stress conditions at 43 degrees C. KNU5377 evidenced a time-dependent increase in hydroperoxide levels, carbonyl contents, and malondialdehyde (MDA), which increased in the expression of a variety of cell rescue proteins containing Hsp104p, Ssap, Hsp30p, Sod1p, catalase, glutathione reductase, G6PDH, thioredoxin, thioredoxin peroxidase (Tsa1p), Adhp, Aldp, trehalose and glycogen at high temperature. Pma1/2p, Hsp90p and H+-ATPase expression levels were reduced as the result of exposure to heat shock. With regard to cellular fatty acid composition, levels of unsaturated fatty acids (USFAs) were increased significantly at high temperatures (43 degrees C), and this was particularly true of oleic acid (C18:1). The results of this study indicated that oxidative stress as the result of heat shock may induce a more profound stimulation of trehalose, antioxidant enzymes, and heat shock proteins, as well as an increase in the USFAs ratios. This might contribute to cellular protective functions for the maintenance of cellular homeostasis, and may also contribute to membrane fluidity. SN - 1225-8873 UR - https://www.unboundmedicine.com/medline/citation/17082742/Heat_shock_causes_oxidative_stress_and_induces_a_variety_of_cell_rescue_proteins_in_Saccharomyces_cerevisiae_KNU5377_ L2 - https://biocyc.org/gene?orgid=YEAST&id=G3O-33950 DB - PRIME DP - Unbound Medicine ER -