Open AccessA non‐covalent NH 2 ‐terminal pro‐region aids the production of active aqualysin I (a thermophilic protease) without the COOH‐terminal pro‐sequence in Escherichia coli
Author(s) -
Lee YoungChoon,
Ohta Takahisa,
Matsuzawa Hiroshi
Publication year - 1992
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.1574-6968.1992.tb05238.x
Subject(s) - thermus , escherichia coli , protease , thermus aquaticus , signal peptide , sequence (biology) , peptide sequence , biology , thermophile , biochemistry , consensus sequence , active site , microbiology and biotechnology , enzyme , gene
The precursor of aqualysin I, an extracellular protease produced by Thermus aquaticus , consists of four domains: an N‐terminal signal peptide, an N‐terminal pro‐sequence, the protease domain and a C‐terminal pro‐sequence. In an Escherichia coli expression system, mature and active aqualysin I is formed by treatment at 65°C and the N‐pro‐sequence is required for its production. Complete deletion of the C‐prosequence did not affect the production of active aqualysin I, indicating that the C‐pro‐sequence is not essential. A non‐covalent N‐pro‐region was separately synthesized from the protease domain with or without the C‐pro‐sequence. In this system, mature and active aqualysin I was detected only when the C‐pro‐sequence was deleted.