title: A non-covalent NH2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli.
abstract: 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 degrees C and the N-pro-sequence is required for its production. Complete deletion of the C-pro-sequence 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.
authors.affiliation: Department of Agricultural Chemistry, University of Tokyo, Japan.
authors.forename: Y C
authors.initials: YC
authors.lastname: Lee
authors.forename: T
authors.initials: T
authors.lastname: Ohta
authors.forename: H
authors.initials: H
authors.lastname: Matsuzawa
mesh_terms: D001483:Base Sequence; D004252:DNA Mutational Analysis; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis; D012697:Serine Endopeptidases / Q000096:biosynthesis* / Q000235:genetics; D013329:Structure-Activity Relationship; D013824:Thermus / Q000235:genetics*
chemical_list: D011994:Recombinant Proteins; D012697:Serine Endopeptidases; C055102:aqualysin I