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Lipase gene from Pseudomonas species is followed with an accessory gene called lipase activator gene, which is necessary for the production and excretion of mature lipase. The biochemical function of the activator gene has remained undetermined. Our group has isolated the activator gene, lipB, with lipase gene, lipA, from Pseudomonas aeruginosa TE 3285. Although lipA was expressed in Escherichia coli and its signal peptide was correctly processed at the same position as in Pseudomonas, the mature lipase deposited as inactive, inclusion bodies in E. coli cells. The lipase activity of the inclusion bodies did not recover by solubilization with urea. To gain lipase activity, solubilization required the fusion protein of lipB protein with glutathione S-transferase. The mode of the reactivation is different from chaperones and rather similar to intramolecular chaperones.

Identification of Biochemical Function of Lipase Activator Gene (lipB) from Pseudomonas aeruginosa TE 3285