Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL

Abstract

In the dense cellular environment, protein misfolding and inter-molecular protein aggregation compete with protein folding. Chaperones associate with proteins to prevent misfolding and to assist in folding to the native state. In Escherichia coli, the chaperones trigger factor, DnaK/DnaJ/GrpE, and GroEL/ES are the major chaperones responsible for insuring proper de novo protein folding. With multitudes of proteins produced by the bacterium, the chaperones have to be selective for their substrates. Yet, chaperone selectivity cannot be too specific. Recent biochemical and high-throughput studies have provided important insights highlighting the strategies used by chaperones in maintaining proteostasis in the cell. Here, we discuss the substrate networks and cooperation among these protein folding chaperones.

Keywords: Chaperone interaction network; DnaK/DnaJ/GrpE; GroEL/GroES; Molecular chaperones; Protein aggregation; Protein folding; Trigger factor.