Abstract
Heat shock proteins (Hsps) are frequent targets to be manipulated in Escherichia coli (E. coli) to improve the production of recombinant proteins and secondary metabolites for industrial applications. In this study, we examined if the heterologous expression of eukaryotic Hsps can effectively enhance bacterial growth, compared to overexpression of endogenous bacterial Hsps. Five transgenic E. coli cell lines (TCs), individually expressing recombinant bacterial Hsps (IbpA, IbpB, and DnaK) and plant Hsps [carrot (Daucus carota L.: Dc) Hsp17.7 and Hsp70], were generated to compare the growth-enhancing effect of each protein. Under normal and heat conditions, the TC expressing DcHsp17.7 showed the highest growth rate and maximum cell density. Under cold, acetate, and ethanol conditions, the TC overexpressing IbpA showed the highest growth rate. TCs expressing Hsps showed higher protein levels than the control. The amino acid sequence comparison shows that bacterial and plant small(s) Hsps are less conserved than larger Hsp70s. Conserved 13 a.a. sequences in the N-terminal domain of plant sHsps were not present in the bacterial IbpA and IbpB, suggesting possible differences in the functions of plant and bacterial sHsps. Results show that different Hsps could be employed to maximize bacterial cell growth for varied industrial applications.
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