Involvement of NH_2-Terminal Pro-sequence in the Production of Active Aqualysin I (a Thermophilic Serine Protease) in Escherichia coli(Biological Chemistry)

概要

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Aqualysin I is a heat-stable subtilisin-type protease produced by Thermus aquaticus YT-1. The precursor of aqualysin I consists of four domains: an NH_2-terminal signal peptide, an NH_2-terminal pro-sequence, a protease domain, and a COOH-terminal pro-sequence. In Escherichia coli cells harboring recombinant plasmid carrying the aqualysin I gene, proteolytic activity is obtained on treatment at 65℃ and mature enzyme is detected. In the case of mutant genes containing partial deletions in the NH_2-terminal pro-sequence, no proteolytic activity was detected and the precursor protein was found to be unstable in E. coli. These results indicate that the NH_2-terminal pro-sequence is required to produce the active enzyme by stabilizing the precursor structure. Amino acid substitutions in the conserved sequence of the NH_2-terminal pro-sequence found among subtilisin-type proteases made the processing faster compared with the wild type.
社団法人日本農芸化学会の論文
1991-12-23