High-level secretion of human growth hormone by Escherichia coli

Gene. 1987;55(2-3):189-96. doi: 10.1016/0378-1119(87)90279-4.

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 micrograms of hGH/ml/1 A550 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.

MeSH terms

  • Chorionic Gonadotropin / biosynthesis
  • Chorionic Gonadotropin / genetics
  • Chorionic Gonadotropin / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / physiology
  • Genes
  • Genes, Synthetic
  • Genetic Vectors
  • Humans
  • Promoter Regions, Genetic
  • Protein Processing, Post-Translational
  • Protein Sorting Signals / genetics
  • Protein Sorting Signals / physiology
  • Recombinant Fusion Proteins / metabolism*
  • Recombinant Proteins / metabolism*
  • Regulatory Sequences, Nucleic Acid

Substances

  • Chorionic Gonadotropin
  • Protein Sorting Signals
  • Recombinant Fusion Proteins
  • Recombinant Proteins