Interaction of HSP 70 Family with Native and Denatured Proteins

众所周知，所有细胞都会短暂地增加一组蛋白质的表达——热休克或应激蛋白——以应对各种施加的压力。虽然hsp70家族最近被认为是蛋白质成熟事件的必要因素，但这些蛋白在非应激细胞中以降低但重要的水平存在，其功能在很大程度上是未知的。计划的工作将集中于hsps70在体内和体内的推定相互作用，重点关注ATP在靶标结合/释放中的作用，以及靶蛋白的命运；评估可能与hsp70相互作用的预先存在的蛋白质的数量和类型，作为应激的函数，以及与耐热性的关系将被研究。这样的研究将导致对热休克蛋白在正常细胞事件和伴随应激反应的细胞事件中的功能有更全面的理解。细胞对各种压力的反应——热、重金属污染、压力等——涉及到某些蛋白质合成水平的提高，这些蛋白质被称为热休克蛋白；这些蛋白与其他细胞蛋白的相互作用将被研究，作为了解这些热休克蛋白在正常细胞和应激细胞中所起确切作用的努力的一部分。//

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. //