The use of the Xenopus oocyte as a model system to analyze the expression and function of eukaryotic heat shock proteins

The analysis of the expression and function of heat shock protein (lisp) genes, a class of molecular chaperones, has been greatly aided by studies carried out with Xenopus oocytes. The large size of the oocyte facilitates microinjection of DNA, mRNA or protein, permits manual dissection of nuclei, and allows certain assays to be performed with single oocytes. These and other characteristics were useful in identifying the cis- and trans-acting factors involved in lisp gene transcription as well as the role of chaperones and co-chaperones in the repression and activation of heat shock factor. Xenopus oocytes were used to examine heat shock protein (HSP) molecular chaperone function as well as their involvement in intracellular trafficking, maturation, and secretion of protein. Possible new areas of research with this system include the role of membranes in the heat shock response, involvement of HSPs in viral replication and maturation, and in vivo NMR spectroscopy of microinjected HSPs. (c) 2007 Elsevier Inc. All rights reserved.