Role of chaperones and a cytoplasmatic protease in recombinant protein production in E. coli at suboptimal growth temperature

Recent studies have revealed that at lower cultivation temperatures (25°C) much higher percentage of correctly folded recombinant proteins can be extracted from inclusion bodies. The goal of our research was to investigate mechanisms determining characteristics of non-classical inclusion bodies production using gene expression profiling. Two strains of recombinant E. coli [BL21 (DE3)] grown at three different temperatures (25°C, 37°C and 42°C) were included in experiment. Gene expression was studied in two recombinant strains (production and control strain), grown at three different temperatures (25, 37 and 42 oC) in three biological replicates. Cells were harvesed at OD=4, except for the cells grown at 25 oC, here they were harvested at OD=4 and OD=10.