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首页> 外文期刊>Molecular and Cellular Biology >Proteasome Inhibitors Cause Induction of Heat Shock Proteins and Trehalose, Which Together Confer Thermotolerance inSaccharomyces cerevisiae
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Proteasome Inhibitors Cause Induction of Heat Shock Proteins and Trehalose, Which Together Confer Thermotolerance inSaccharomyces cerevisiae

机译：蛋白酶体抑制剂引起热休克蛋白和海藻糖的诱导，它们共同赋予酿酒酵母耐热性。

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An accumulation in cells of unfolded proteins is believed to be the common signal triggering the induction of heat shock proteins (hsps). Accordingly, in Saccharomyces cerevisiae, inhibition of protein breakdown at 30°C with the proteasome inhibitor MG132 caused a coordinate induction of many heat shock proteins within 1 to 2 h. Concomitantly, MG132, at concentrations that had little or no effect on growth rate, caused a dramatic increase in the cells’ resistance to very high temperature. The magnitude of this effect depended on the extent and duration of the inhibition of proteolysis. A similar induction of hsps and thermotolerance was seen with another proteasome inhibitor, clasto-lactacystin β-lactone, but not with an inhibitor of vacuolar proteases. Surprisingly, when the reversible inhibitor MG132 was removed, thermotolerance decreased rapidly, while synthesis of hsps continued to increase. In addition, exposure to MG132 and 37°C together had synergistic effects in promoting thermotolerance but did not increase hsp expression beyond that seen with either stimulus alone. Although thermotolerance did not correlate with hsp content, another thermoprotectant trehalose accumulated upon exposure of cells to MG132, and the cellular content of this disaccharide, unlike that of hsps, quickly decreased upon removal of MG132. Also, MG132 and 37°C had additive effects in causing trehalose accumulation. Thus, the resistance to heat induced by proteasome inhibitors is not just due to induction of hsps but also requires a short-lived metabolite, probably trehalose, which accumulates when proteolysis is reduced.
机译：据信，未折叠蛋白在细胞中的积累是触发热激蛋白（hsps）诱导的常见信号。因此，在中，蛋白酶体抑制剂MG132在30℃下抑制蛋白质分解导致在1-2小时内协同诱导许多热激蛋白质。随之而来的是，MG132的浓度对生长速率影响很小或没有影响，导致细胞对极高温度的抵抗力急剧增加。这种作用的程度取决于抑制蛋白水解的程度和持续时间。用另一种蛋白酶体抑制剂 clasto -lactacystinβ-内酯也观察到了类似的hsps诱导和耐热性，而液泡蛋白酶抑制剂则没有。令人惊讶地，当去除可逆抑制剂MG132时，耐热性迅速降低，而hsps的合成继续增加。另外，暴露于MG132和37°C共同具有促进耐热性的协同作用，但没有增加hsp表达，超过了单独使用任一刺激所见的水平。尽管耐热性与hsp含量不相关，但另一种热保护剂海藻糖在细胞暴露于MG132后积累，并且与hsps不同，该二糖的细胞含量在去除MG132后迅速降低。同样，MG132和37℃在引起海藻糖积累方面具有累加作用。因此，蛋白酶体抑制剂诱导的耐热性不仅是由于hsps的诱导，而且还需要一种寿命短的代谢产物，可能是海藻糖，当减少蛋白水解作用时会累积。

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