Open AccessSynthesis and secretion of human epidermal growth factor by Escherichia coli.
Author(s) -
Toshihiko Oka,
Shunji Sakamoto,
Ken Miyoshi,
Tohru Fuwa,
Koji Yoda,
Makari Yamasaki,
Gakuzo Tamura,
Toru Miyake
Publication year - 1985
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.21.7212
Subject(s) - periplasmic space , signal peptide , escherichia coli , alkaline phosphatase , biology , epidermal growth factor , plasmid , secretion , recombinant dna , microbiology and biotechnology , biochemistry , phosphatase , gene , enzyme , receptor
A synthetic gene for human epidermal growth factor (hEGF) was joined to a sequence encoding the signal peptide of Escherichia coli alkaline phosphatase. This hybrid gene was placed under the control of the alkaline phosphatase gene (phoA) promoter in a recombinant plasmid, which was used to transfect E. coli. The hybrid protein that was expressed in host cells under conditions of phosphate limitation was processed accurately during the secretion process, and mature hEGF was recovered in the periplasmic fraction. On the other hand, no EGF was detected in the periplasmic space when the synthetic hEGF gene was not accompanied by the phoA signal sequence.