Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Involvement of NH2-Terminal Pro-sequence in the Production of Active Aqualysin I (a Thermophilic Serine Protease) in Escherichia coli
Young-Choon LEEYuko MIYATAIchiro TERADATakahisa OHTAHiroshi MATSUZAWA
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1991 Volume 55 Issue 12 Pages 3027-3032

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Abstract

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 NH2-terminal signal peptide, an NH2-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°C and mature enzyme is detected. In the case of mutant genes containing partial deletions in the NH2-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 NH2-terminal pro-sequence is required to produce the active enzyme by stabilizing the precursor structure. Amino acid substitutions in the conserved sequence of the NH2-terminal pro-sequence found among subtilisin-type proteases made the processing faster compared with the wild type.

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© Japan Society for Bioscience, Biotechnology, and Agrochemistry
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