Structural and functional organization of the signal peptide of pro-enterotoxin B from Staphylococcus aureus

A series of genes of pro-enterotoxin B from Staphylococcus aureus containing signal peptide mutant forms was constructed in order to study the functional roles of the introduced mutations. It was shown that a continuous mutation in the n-region of the signal peptide does not affect the secretion efficiency of proenterotoxin B, in contrast to the analogous mutation in the h-region. Point mutations of the pro-protein signal peptide, including the N-terminal amino acid residue of the mature protein, were obtained. It was shown that the introduced structural changes cause a decrease in secretion efficiency and a redistribution of the protein in various compartments of Escherichia coli cells.