Heterologous expression of AgsA enhances Escherichia coli tolerance to the combined effect of elevated temperature and Zinc toxicity.

Small heat shock proteins (sHSPs) are ubiquitous stress proteins that are able to protect the cells against cellular insults from temperature, heavy metal etc. However, the molecular chaperone roles of sHSPs in enhancing growth and adaptation under combined temperature and metal stresses in Escherichia coli cells have been poorly understood. Here, we analyze the function of recombinant AgsA, a small heat shock protein from Salmonella enterica serovar Typhimurium under combined temperature and zinc stress in E. coli. Our results show that the heterologous expression of AgsA significantly increases the tolerance of E. coli cells to the combined effect of temperature stress and zinc toxicity by maintaining the stability of soluble proteins. Furthermore, there was remarkable and significant difference in the half effect concentration (EC50) of zinc at all temperatures treatments in both test cells. The EC50s of zinc at 37 °C, 42 °C and 50 °C were 15.24 mg/L, 29.30 mg/L, and 5.98 mg/L respectively in the AgsA-transformed E. coli cells, and 3.03 mg/L, 2.38 mg/L, and 0.373 mg/L, respectively in the control cells lacking AgsA. Together, our data indicate a good concentration-response relationship between all three temperatures treatment and zinc toxicity in E. coli, and establish for the first time the combined effects of temperature and zinc toxicity on E. coli cells. Also, the AgsA protein response to combined thermal and metal stress could serve as a molecular biomarker for the assessment of interactive stress damage to the cells.