Abstract
A gene encoding the mature form of human growth hormone (hGH) was fused to the secretion signal coding sequence of the Escherichia coli heat-stable enterotoxin II (STII). This hybrid gene was preceded by two Shine-Dalgarno sequences derived from the trp and STII-coding genes and was expressed in E. coli under the transcriptional control of the E. coli alkaline phosphatase ( phoA) promoter. In low-phosphate growth media, cells synthesized about 15 to 25 μg of hGH/ml/1 A 550 unit of cells. This represents 6 to 10% of total cellular protein. The majority of the hGH produced (more than 90%) was processed precisely and secreted into the periplasmic space. These results demonstrate that E. coli cells are able to synthesize and secrete high levels of this human protein using a prokaryotic signal sequence.
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