Effect of SecB Chaperone on Production of Periplasmic Penicillin Acylase in Escherichia coli

• Published in: Biotechnology progress Vol. 15; no. 3; pp. 439 - 445
• Main Authors: Chou, C. Perry, Tseng, Jen-Hung, Kuo, Bao-Yuan, Lai, Ko-Ming, Lin, Ming-I, Lin, Hua-Kuo
• Format: Journal Article
• Language: English
• Published: USA American Chemical Society 01.05.1999; American Institute of Chemical Engineers
• Subjects: Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Biological and medical sciences; Biosynthesis; Biotechnology; Chromosomes; Enzymes; Escherichia coli; Escherichia coli - enzymology; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; Gene Expression; Genes, Bacterial; Genetic engineering; Genetic technics; Genetic Vectors; Methods. Procedures. Technologies; Microorganisms; Modification of gene expression level; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Mutation; Penicillin Amidase - biosynthesis; Plasmids - genetics; Stabilization; Penicillin amidase; Enzymatic activity; Enzyme; Stabilization; Chaperone; Escherichia coli; Production; Bacteria; Hydrolases; Precursor; Comparative study; Enterobacteriaceae
• ISSN: 8756-7938; 1520-6033
• DOI: 10.1021/bp990036z

The effect of SecB chaperone on production of periplasmic penicillin acylase (PAC) in Escherichia coli was investigated. It appears that formation of PAC required the function of SecB chaperone and the amount of SecB required was at a basal level. The secB mutant was defective in production of PAC, and the impairment could be complemented by extrachromosomally supplementing SecB in trans. The function of SecB might be primarily stabilizing the cytoplasmic PAC precursors. Overproduction of SecB chaperone usually resulted in an increase in the amount of PAC precursors without enhancing PAC activity. In addition, most of the PAC precursors were located in the periplasm, suggesting that formation of active PAC was likely limited by periplasmic processing steps.