Interaction of HSP 70 Family with Native and Denatured Proteins

已知所有细胞都瞬时增加一种蛋白质的表达， 一组蛋白质--热休克蛋白或应激蛋白--作为反应， 承受各种压力 这些蛋白质已知是 在非应激细胞中以降低但显著的水平存在 在很大程度上，其功能未知，尽管hsp 70家族具有 最近被认为是蛋白质成熟所必需的 事件 计划中的工作将侧重于以下方面的假定相互作用： hsps 70，在体内和体内，重点是ATP的作用， 靶的结合/释放，以及靶蛋白的命运; 评估预先存在的蛋白质的量和类型， 与热休克蛋白70相互作用，作为压力的函数， 将研究耐热性。 这些研究应该导致 对正常细胞中热休克蛋白功能的再认识 事件，以及伴随压力反应的事件。 细胞对各种压力的反应热重金属 污染，压力等等--涉及更高水平的 某些称为热休克蛋白的蛋白质的合成; 这些蛋白质与其他细胞蛋白质的相互作用， 作为努力理解这些确切作用的一部分， 热休克蛋白在正常和应激细胞中发挥作用。//

All cells are known to transiently increase the expression of a group of proteins--the heat shock or stress proteins--in response to a variety of imposed stresses. These proteins, known to be present at reduced, but significant, levels in non-stressed cells are of, largely, unknown function, although the hsp70 family have been implicated recently as essential for protein maturation events. The work planned will focus on putative interactions of hsps70, both in vivo and in vivo, focusing on the role of ATP in binding/release of targets, and in the fate of targeted proteins; evaluation of amounts and types of pre-existing proteins that may interact with hsp70, as a function of stress, and the relationship to thermotolerance will be studied. Such studies should lead to a fuller comprehension of the functions of hsps in normal cell events, and in those that accompany stress responses. The cellular responses to a variety of stresses--heat, heavy metal contamination, pressure, etc.--involve an increased level of synthesis of certain proteins designated heat-shock-proteins; the interactions of these proteins with other cell proteins will be examined as part of an effort to understand the precise role these heat shock proteins play in normal, as well as stressed, cells. //