Intracellular form of streptococcal proteinase: a clue to a novel mechanism of secretion.
The intracellular form of streptococcal proteinase has been isolated and compared with its extracellular form. As shown by double-immunodiffusion studies and radiosequence analysis, the intracellular proteinase was identical to that of the extracellular proteinase. However, the unusual mixed disulfide, protein-S-SR, shown to be present in the extracellular proteinase, was missing in the intracellular proteinase. Protease activity is dependent upon the free sulfhydryl group of the proteinase. Thus, the intracellular proteinase was enzymatically active, while the extracellular proteinase requires activation by exposure to a reducing agent. Because this appears to be the only difference between the intracellular and extracellular protease, it is proposed that the modification of the protein-SH to form protein-S-SR is a process that is intimately related to the mechanism of secretion of the proteinase into the culture fluid by streptococci.
D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D010450:Endopeptidases / Q000032:analysis*; D005779:Immunodiffusion; D008239:Lysine / Q000032:analysis; D013291:Streptococcus / Q000201:enzymology*
D000596:Amino Acids; D010450:Endopeptidases; D008239:Lysine