高等植物热激转录因子生物学特性及其在非生物胁迫适应中的作用

热激转录因子(HSFs)参与了植物生长发育的调控以及多种非生物胁迫适应基因的表达调控。HSFs通常形成同源三聚体,激活转录活性从而发挥功能。本文综述了热激转录因子的基本结构、亚细胞定位、转录调控、功能多样性及其在植物适应极端温度、盐害、干旱、强光和氧化胁迫等非生物胁迫过程中的作用。HSFs是提高高等植物抗多重胁迫的优质候选基因,对其深入研究具有重要的应用价值。未来,通过生物基因工程等手段利用HSFs提高各类作物抗性具有广阔的发展前景。     

人热休克因子1突变体的应用研究进展

热休克因子1是调节应激反应的主要转录因子,它在应激条件下可被活化。通过基因突变得到正显性和负显性热休克因子1,它们不需要外界条件刺激就分别具有启动热休克蛋白的表达或竞争抑制内源热休克因子1活性的能力。目前,已有多个热休克因子1的突变体应用于疾病研究。介绍了热休克因子1的结构和活化途径,以及热休克因子1突变体在肿瘤、神经系统及心血管系统等方面的应用进展。     

Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27

Protein kinase B (PKB, also named as Akt or RAC-protein kinase), that is activated by cellular stress such as heat shock and hyperosmotic treatment, was revealed to be activated by oxidative stress and by chemical stressors of CdCl₂ and NaAsO₂ by measuring the activity of the enzyme immunoprecipitated from the transfected COS-7 cells. Upon stress treatment, a 30-kDa phosphoprotein was co-immunoprecipitated with PKB from the cells metabolic labeled with [³²P]orthophosphate. The phosphoprotein was identified as Hsp27, a small heat shock protein, by immunoblot analysis and co-immunoprecipitation. The association of Hsp27 was specific to PKB as the heat shock protein was not co-immunoprecipitated with other protein kinases such as protein kinase C and PKN. When the cells were treated with H₂O₂, PKB was activated gradually and the association of Hsp27 with PKB increased concurrently with the enhancement of PKB activity. In heat-shocked cells, activation of PKB and the association of Hsp27 were detected immediately after the treatment, and the association of the heat shock protein decreased while PKB kept stimulated activity when the cells were further incubated at 37°C. These results suggest that Hsp27 is involved in the activation process of PKB in the signal transduction pathway of various forms of stress.