[Localization of acid phosphatase in Saccharomyces cerevisiae and its export into culture media depends on the type of the N-terminal signal peptide].

The aim of this work was to study the character of intracellular distribution and efficiency of yeast acid phosphatase export depending on the type of the N-terminal signal peptide used. A number of plasmids carrying the acid phosphatase genes with different signal peptides sequences was constructed. The main site of the enzyme accumulation for the variant containing its own acid phosphatase signal peptide was the periplasm. Approximately the same pattern was observed when the hybrid signal peptide consisting of acid phosphatase signal peptide and alpha-factor preprosegment tandem was used. Unlike the above-mentioned systems the strain carrying acid phosphatase under the control of alpha factor preprosegment was able to export the enzyme into the culture medium. The experiments have shown the possibility of changing the final localization of secretory proteins by replacing the N-terminal signal peptide.