Voellmy R
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, FL 33101, USA.
EXS. 1996;77:121-37. doi: 10.1007/978-3-0348-9088-5_9.
Heat shock protein gene expression is enhanced by proteotoxic stress, i.e., by conditions favoring protein unfolding. This upregulation of heat shock protein genes is mediated by heat shock transcription factor HSF1. A mechanism, the details of which are still elusive, senses adverse conditions and causes HSF1 to oligomerize and to acquire DNA-binding ability. The DNA-binding form of HSF1 then undergoes further conformational changes that render it transcriptionally competent. The current model in which heat shock protein 70 acts both as sensor of stress and as negative regulator of HSF1 oligomerization as well as alternative models involving additional protein factors are discussed.
热休克蛋白基因表达通过蛋白毒性应激增强，即通过有利于蛋白质解折叠的条件增强。热休克蛋白基因的这种上调由热休克转录因子HSF1介导。一种机制（其细节仍不清楚）感知不利条件并导致HSF1寡聚化并获得DNA结合能力。HSF1的DNA结合形式随后经历进一步的构象变化，使其具有转录活性。文中讨论了热休克蛋白70既作为应激传感器又作为HSF1寡聚化负调节剂的当前模型以及涉及其他蛋白质因子的替代模型。
