2008
DOI: 10.2478/s11658-007-0033-y
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The effect of calnexin deletion on the expression level of PDI in Saccharomyces cerevisiae under heat stress conditions

Abstract: Abstract:We cultured calnexin-disrupted and wild-type Saccharomyces cerevisiae strains under conditions of heat stress. The growth rate of the calnexin-disrupted yeast was almost the same as that of the wild-type yeast under those conditions. However, the induced mRNA level of the molecular chaperone PDI in the ER was clearly higher in calnexin-disrupted S. cerevisiae relative to the wild type at 37ºC, despite being almost the same in the two strains under normal conditions. The western blotting analysis for P… Show more

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Cited by 6 publications
(4 citation statements)
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“…In this study, the expression of protein disulfide isomerase A4 (PDIA4) was upregulated to promote correct protein folding. PDI may interact to recover part of the function of CNX, thus promoting the recovery and maintenance of normal lung function in yaks under high-altitude conditions 36 . The misfolded proteins in the ER lumen are recognized by luminal chaperones such as HSP40, NEF, GRP94 and BIP, which transfer misfolded proteins to the ER membrane for ubiquitin-dependent degradation (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…In this study, the expression of protein disulfide isomerase A4 (PDIA4) was upregulated to promote correct protein folding. PDI may interact to recover part of the function of CNX, thus promoting the recovery and maintenance of normal lung function in yaks under high-altitude conditions 36 . The misfolded proteins in the ER lumen are recognized by luminal chaperones such as HSP40, NEF, GRP94 and BIP, which transfer misfolded proteins to the ER membrane for ubiquitin-dependent degradation (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…It appears that the deletion of calnexin results in the induction of the unfolded protein response (UPR), and increases the levels of PDI and BiP to fold the unfolded glycosylated lysozymes (internal stress) [13]. We found that the induction of PDI in the ER could recover part of the function of calnexin in calnexin-disrupted yeast under heat stress conditions [14]. BiP, unlike PDI, which directly interacts with calnexin, was also found to cooperate with calnexin in the ATP-dependent refolding of glycoprotein and non-glycosylated substrates [15].…”
Section: Introductionmentioning
confidence: 83%
“…Как уже было сказано, Pdi -мультифункциональный белок и может действовать в клетке и как фермент, и как шаперон. Есть данные, что Pdi в условиях теплового стресса может брать на себя часть функций шаперона ЭР -калнексина [43]. Полученные данные позволяют предположить, что повышенная продукция Pdi оказывает влияние на различные внутриклеточные процессы.…”
Section: Discussionunclassified