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- 검색키워드
- 저자 : Mahendran Chinnamara Naicker (검색결과 2 건)
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Identification of Chaperones in Freeze Tolerance in Saccharomyces cerevisiae
Mahendran Chinnamara Naicker,조이슬,임하나 한국미생물학회 2012 The journal of microbiology Vol.50 No.5
Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins. Considering the roles played by chaperones in facilitating protein folding and preventing protein aggregation, chaperones must exist that confer tolerance to cold stress. Here, yeast strains lacking individual chaperones were screened for reduced freezing tolerance. In total, 19 of 82 chaperone-deleted strains tested were more sensitive to freeze-thaw treatment than wild-type cells. The reintroduction of the respective chaperone genes into the deletion mutants recovered the freeze tolerance. The freeze sensitivity of the chaperone-knockout strains was also retained in the presence of 20% glycerol.
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Yeast Cyclophilins Prevent Cold Denaturation of Proteins
Mahendran Chinnamara Naicker,김양희,이경희,임하나 대한화학회 2016 Bulletin of the Korean Chemical Society Vol.37 No.3
Freezing environments are one of the major challenges faced by many organisms, including Saccharomyces cerevisiae. Exposure to low temperatures reduces protein folding rates and induces the cold denaturation of proteins, necessitating aid from chaperones. In a previous study, we identified 19 chaperone genes, the deletion of which makes the host more vulnerable to freeze-and-thaw treatments. Among those, peptidyl–prolyl cis–trans isomerases (PPIases) were the most frequently identified. At low temperatures, peptidyl–prolyl isomerization is a rate-limiting step in protein folding, and folding intermediates, which are prone to protein aggregation, tend to accumulate. To characterize their mode of function, the identified PPIases were overexpressed in Escherichia coli. Not only did they increase the survival of E. coli during freeze-and-thaw treatment at –20 °C, but they also protected β-galactosidase against freeze-induced protein denaturation. Purified Cpr1p facilitated the refolding of a slow-folding substrate protein in vitro. These results suggest that the identified PPIases enhance cold survival of cells by preventing cold-induced protein denaturation and promoting protein folding.
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