Parsell D A, Sanchez Y, Stitzel J D, Lindquist S
Howard Hughes Medical Institute, University of Chicago, Illinois 60637.
Nature. 1991 Sep 19;353(6341):270-3. doi: 10.1038/353270a0.
Most eukaryotic cells produce proteins with relative molecular masses in the range of 100,000 to 110,000 after exposure to high temperatures. These proteins have been studied only in yeast and mammalian cells. In Saccharomyces cerevisiae, heat-shock protein hsp104 is vital for tolerance to heat, ethanol and other stresses. The mammalian hsp110 protein is nucleolar and redistributes with growth state, nutritional conditions and heat shock. The relationships between hsp110, hsp104 and the high molecular mass heat-shock proteins of other organisms were unknown. We report here that hsp104 is a member of the highly conserved ClpA/ClpB protein family first identified in Escherichia coli and that additional heat-inducible members of this family are present in Schizosaccharomyces pombe and in mammals. Mutagenesis of two putative nucleotide-binding sites in hsp104 indicates that both are essential for function in thermotolerance.
大多数真核细胞在暴露于高温后会产生相对分子质量在100,000至110,000范围内的蛋白质。这些蛋白质仅在酵母和哺乳动物细胞中得到研究。在酿酒酵母中，热休克蛋白hsp104对于耐热、耐乙醇及其他应激至关重要。哺乳动物的hsp110蛋白位于核仁，会随生长状态、营养条件和热休克而重新分布。hsp110、hsp104与其他生物体的高分子量热休克蛋白之间的关系尚不清楚。我们在此报告，hsp104是首先在大肠杆菌中鉴定出的高度保守的ClpA/ClpB蛋白家族的成员，并且该家族的其他热诱导成员存在于粟酒裂殖酵母和哺乳动物中。hsp104中两个推定的核苷酸结合位点的诱变表明，两者对于耐热性功能均必不可少。
