Microarray-based analysis of recombinant protein production in E.coli

The production of heterologous proteins in E. coli is a powerful tool in the generation of many important biotechnological and medical products. Despite its widespread use as an expression host, however, yields of correctly folded, functional protein are frequently low in E. coli. This is due largely to the formation of insoluble protein aggregates and to premature lysis of the bacterial cells. We, and others, have previously shown that the cell lysis phenomenon associated with recombinant protein production in E. coli is not a direct result of synthesis of heterologous proteins [1], [2]. Instead, protein production triggers a global stress response in the bacterium, but the mechanism by which cell lysis subsequently occurs remains unclear [3]