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[酿酒酵母原生质体中热休克蛋白的合成]

[Synthesis of heat-shock proteins in Saccharomyces cerevisiae protoplasts].

作者信息

Bekker M L, Akhmedov A T, Smolina V S, Naryzhnyĭ S N

出版信息

Mol Gen Mikrobiol Virusol. 1989 May(5):15-9.

PMID:2664488
Abstract

The effect of cellular capsule elimination in Saccharomyces cerevisiae yeasts (protoplast formation) on the heat-shock protein synthesis and the synthesis of the proteins in protoplasts were studied. The methods of mono- and dimeric electrophoresis have demonstrated that (1) about 18 heat-shock proteins with the molecular masses 26-98 Kd are synthesized in cells at 41 degrees C; (2) protoplast formation per se does not induce the synthesis of heat-shock proteins, but the induction of these proteins in protoplasts at 41 degrees C is similar to the one in intact cells. The protoplast formation induces the synthesis of specific proteins different from heat-shock proteins and the synthesis is inhibited by the heat-shock. The heat-shock induces modification of 88 and 86 Kd heat-shock proteins. It inhibits the synthesis of a number of peptides (15-50 Kd) in cells and protoplasts.

摘要

研究了酿酒酵母中细胞胶囊消除(原生质体形成)对热休克蛋白合成以及原生质体中蛋白质合成的影响。单聚体和二聚体电泳方法表明:(1)在41摄氏度时,细胞中合成了约18种分子量为26 - 98千道尔顿的热休克蛋白;(2)原生质体形成本身不会诱导热休克蛋白的合成,但在41摄氏度时原生质体中这些蛋白的诱导情况与完整细胞中的相似。原生质体形成诱导了不同于热休克蛋白的特定蛋白质的合成,且该合成受到热休克的抑制。热休克诱导了88千道尔顿和86千道尔顿热休克蛋白的修饰。它抑制细胞和原生质体中多种肽(15 - 50千道尔顿)的合成。

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