Hyperproduction of araC protein from Escherichia coli

Abstract

Hypersynthesis of araC orotein from E. coli was accomplished. The araC gene was cloned on plasmid pBR322 and some of the noncoding DNA preceding the araC gene was removed by exonuclease digestion. A DNA fragment containing the lac promoter and ribosome binding site was placed in front the araC gene. By these means, the level of araC protein was increased about 5000-fold above the levels found in wild-type cells. This level of protein permits straightforward purification of sizeable quantities of araC protein.