Pathways of Protein Remodeling by Escherichia Coli Molecular Chaperones

A new concept in molecular biology that has evolved over the past ten years is that proteins fold with assistance from other proteins, collectively referred to as molecular chaperones. All organisms, from bacteria to humans, possess several classes of highly conserved molecular chaperones, defined generally as proteins that bind to non-native conformations of proteins and facilitate correct folding and to native proteins and promote refolding. Extensive work has shown that the function as well as the structure of chaperones are highly conserved and the results obtained from studies of one organism are usually applicable to other organisms (1–3). This review will focus on several ATP-dependent molecular chaperone systems in Escherichia coli, including (i) DnaK, and its co-chaperones, DnaJ and GrpE, (ii) Clp proteins and (iii) GroEL and its co-chaperone, GroES (summarized in Table 1).