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In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. One class of stress proteins, termed the Hsp70 family, is comprised of multiple members, all of which bind ATP in vitro, but which are localized within different intracellular compartments. These include: i) Hsc70 (or constitutive form) present within the cytosol/nucleus; ii) Hsp70 (inducible form) present within the cytosol/nucleus/nucleolus; iii) the constitutive glucose-regulated 78 kDa (or BiP) protein present within the lumen of the endoplasmic reticulum; and iv) the constitutive glucose regulated 75 kDa protein present within the mitochondrial matrix. Members of the Hsp70 family are thought to function as molecular chaperones, assisting in the folding of other proteins in various intracellular compartments. Grp75 is localized in the mitochondrial matrix, where, in concert with Hsp60, is thought to participate in the re-folding of proteins translocated into this organelle. Like its E. coli homolog DnaK, Grp75 possesses a cation-dependent ATPase activity thought to be central to its function as a chaperone.


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