Interaction of HSP 70 Family with Native and Denatured Proteins

众所周知，所有细胞在应对各种压力时，都会瞬间增加一组蛋白质的表达--热休克或应激蛋白质。这些已知在非应激细胞中水平降低但意义重大的蛋白质，其功能在很大程度上是未知的，尽管HSP70家族最近被认为是蛋白质成熟事件的关键。计划的工作将集中在HSP70在体内和体内的假定相互作用，重点是ATP在结合/释放靶标和靶蛋白命运中的作用；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。这样的研究应该有助于更全面地理解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。细胞对各种压力--热、重金属污染、压力等--的反应涉及某些蛋白质合成水平的增加，这些蛋白质被称为热休克蛋白质；这些蛋白质与其他细胞蛋白质的相互作用将被研究，作为努力了解这些热休克蛋白质在正常细胞和应激细胞中所起的确切作用的一部分。//

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. //