EXPRESSION OF RECOMBINATED PROTEINS AND F ORMATION OF INCLUSION-BODIES IN ESCHERICHIA-COLI

Recent developments in the expression of protein in E. coli have resul ted in the availability of techniques that make possible the expressio n of heterologous proteins in a soluble form, a secreted form, as memb rane-bound proteins, and as aggregated inclusion granules. However, th e mechanism which dictates whether the protein is soluble or is aggreg ated, is poorly understood. This review presents the current, and some times cotradictory, knowledge of the formation of inclusion bodies in E. coli.