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. //
