Molecular Chaperones: Their Potential Use in the Production of Recombinant Proteins

Abstract

Protein folding and association depend on the pre-existence of molecular chaperones. These are proteins which facilitate the proper folding of newly synthesized polypeptides by preventing aggregation. Production of recombinant eukaryotic proteins in bacteria often results in the formation of inclusion bodies which contain insoluble, aggregated, inactive forms of the recombinant protein. One recent strategy employed to prevent the formation of aggregated recombinant proteins upon expression in bacteria is through their co-expression with bacterial molecular chaperones. This article reviews the major classes of molecular chaperones found in the cell and their potential use in the production of soluble, functional recombinant protein.