Bohen S P, Yamamoto K R
Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.
Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11424-8. doi: 10.1073/pnas.90.23.11424.
The 90-kDa heat shock protein Hsp90 represents a highly conserved strongly expressed gene family; in Saccharomyces cerevisiae, Hsp90 proteins are essential for cell viability. Hsp90 interacts with certain cellular proteins, including steroid hormone receptors, tyrosine and serine/threonine kinases, and other heat shock proteins, but its biological functions are not understood. The unliganded glucocorticoid receptor must interact with Hsp90 to acquire competence for high-affinity hormone binding and subsequent transcriptional regulation. By screening in yeast for defects in glucocorticoid receptor function, Hsp90 mutants were isolated. Four such mutants are described, all of which interact with the glucocorticoid receptor but display distinct defects in ligand responsiveness and differences in growth and resistance to high temperature.
90千道尔顿热休克蛋白Hsp90代表一个高度保守且强表达的基因家族；在酿酒酵母中，Hsp90蛋白对细胞活力至关重要。Hsp90与某些细胞蛋白相互作用，包括类固醇激素受体、酪氨酸和丝氨酸/苏氨酸激酶以及其他热休克蛋白，但其生物学功能尚不清楚。未结合配体的糖皮质激素受体必须与Hsp90相互作用，以获得高亲和力激素结合和随后转录调控的能力。通过在酵母中筛选糖皮质激素受体功能缺陷，分离出了Hsp90突变体。描述了四个这样的突变体，它们都与糖皮质激素受体相互作用，但在配体反应性方面表现出明显缺陷，在生长和对高温的抗性方面也存在差异。
