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Protein Engineering, Vol. 15, No. 4, 337-345, April 2002
© 2002 Oxford University Press

Engineering a novel secretion signal for cross-host recombinant protein expression

Nguan Soon Tan1,2, Bow Ho3 and Jeak Ling Ding1,4

1 Department of Biological Sciences and 3 Department of Microbiology, National University of Singapore, Singapore 117543

Protein secretion is conferred by a hydrophobic secretion signal usually located at the N-terminal of the polypeptide. We report here, the identification of a novel secretion signal (SS) that is capable of directing the secretion of recombinant proteins from both prokaryotes and eukaryotes. Secretion of fusion reporter proteins was demonstrated in Escherichia coli, Saccharomyces cerevisiae and six different eukaryotic cells. Estrogen-inducibility and secretion of fusion reporter protein was demonstrated in six common eukaryotic cell lines. The rate of protein secretion is rapid and its expression profile closely reflects its intracellular concentration of mRNA. In bacteria and yeast, protein secretion directed by SS is dependent on the growth culture condition and rate of induction. This secretion signal allows a flexible strategy for the production and secretion of recombinant proteins in numerous hosts, and to conveniently and rapidly study protein expression.


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J. Wang, N. S. Tan, B. Ho, and J. L. Ding
Modular Arrangement and Secretion of a Multidomain Serine Protease. EVIDENCE FOR INVOLVEMENT OF PROLINE-RICH REGION AND N-GLYCANS IN THE SECRETION PATHWAY
J. Biol. Chem., September 20, 2002; 277(39): 36363 - 36372.
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