Abstract
A short synthetic signal peptide (SSSP) of 26 amino acid and a long one of 35 amino acids (LSSP), having an additional ribosome binding site (RBS), were synthesized. The SSSP sequence was based on the comparison of known efficient Streptomycessignal sequences. The SSSP and the LSSP were connected to the Streptomycessp. TO1 amylase gene (amyTO1) without its signal peptide. These constructions, when cloned into Streptomycessp. TO1 and placed under the control of the ermE-up promoter of Saccharopolyspora erythrea, increased the secretion of the amylase up to six-fold when compared to the natural amyTO1 signal peptide.
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Mhiri, S., Mezghani, M., Mellouli, L. et al. Efficient synthetic signal peptides for Streptomyces. Biotechnology Letters 22, 1305–1310 (2000). https://doi.org/10.1023/A:1005678311475
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DOI: https://doi.org/10.1023/A:1005678311475