Munich Center for Integrated Protein Science, Technische Universität München, Department Chemie, Lichtenbergstrasse 4, 85747 Garching, Germany.
Mol Cell. 2010 Aug 27;39(4):507-20. doi: 10.1016/j.molcel.2010.08.001.
Hsp12 of S. cerevisiae is upregulated several 100-fold in response to stress. Our phenotypic analysis showed that this protein is important for survival of a variety of stress conditions, including high temperature. In the absence of Hsp12, we observed changes in cell morphology under stress conditions. Surprisingly, in the cell, Hsp12 exists both as a soluble cytosolic protein and associated to the plasma membrane. The in vitro analysis revealed that Hsp12, unlike all other Hsps studied so far, is completely unfolded; however, in the presence of certain lipids, it adopts a helical structure. The presence of Hsp12 does not alter the overall lipid composition of the plasma membrane but increases membrane stability.
酵母的 Hsp12 在应对应激时会被上调数十倍。我们的表型分析表明，该蛋白对多种应激条件（包括高温）下的生存至关重要。在没有 Hsp12 的情况下，我们观察到应激条件下细胞形态发生变化。令人惊讶的是，在细胞内，Hsp12 既存在于可溶性细胞质蛋白中，也存在于质膜上。体外分析表明，与迄今为止研究的所有其他 Hsp 不同，Hsp12 完全展开；然而，在某些脂质存在的情况下，它会采用螺旋结构。Hsp12 的存在不会改变质膜的总体脂质组成，但会增加膜的稳定性。
