Open AccessRole of the COOH‐terminal pro‐sequence of aqualysin I (a heat‐stable serine protease) in its extracellular secretion by Thermus thermophilus
Author(s) -
Kim DongWook,
Lee YoungChoon,
Matsuzawa Hiroshi
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12750.x
Subject(s) - thermus thermophilus , extracellular , serine protease , secretion , biology , thermus , thermus aquaticus , plasmid , serine , biochemistry , subtilisin , protease , enzyme , microbiology and biotechnology , thermophile , escherichia coli , gene
Aqualysin I is a subtilisin‐type serine protease secreted into the medium by Thermus aquaticus YT‐1. Thermus thermophilus cells harboring a plasmid for the aqualysin I precursor secreted pro‐aqualysin I with the C‐terminal pro‐sequence into the culture medium, and the precursor was then processed to the mature enzyme during the cultivation. However, the extracellular levels of aqualysin I in T. thermophilus cells harboring plasmids for deletion mutants as to the C‐terminal pro‐sequence were about 10–20% in comparison with the level of wild‐type. Only the mature enzyme could be detected in the medium, while pro‐aqualysin I with the C‐terminal pro‐sequence could not. These results suggest that the C‐terminal pro‐sequence of aqualysin I plays an important role in the extracellular secretion of aqualysin I.