Streptokinase secretion by Serratia marcescens signaled by the C-terminal 41 amino acid segment of metalloprotease.

In order to investigate the secretion signal of Serratia marcescens metalloprotease (SMP) and examine the ability of the secretion signal to secrete foreign proteins, hybrid genes encoding the passenger-SMP C-terminal segments were constructed. As a passenger protein, streptokinase (SK) deprived of its signal peptide was used. Three kinds of SMP C-terminal segments containing 41, 80, or 220 amino acid residues were fused to the C-terminus of SK as secretion signals. The SK-SMP chimeric proteins containing 41 or 220 amino acid segments of the SMP C-terminus were secreted into the culture medium by the SMP transporter of S. marcescens. This result suggests that cytoplasmic SK is secreted into the external medium by the C-terminal segments of SMP and also shows that the smallest, 41 amino acid segment of the SMP C-terminus functions as a secretion signal of foreign proteins as well as SMP.