Role of DegP protease on levels of various forms of colicin A lysis protein

• Published in: FEMS microbiology letters Vol. 125; no. 2‐3; pp. 173 - 178
• Main Author: Cavard, Danièle
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 15.01.1995; Blackwell
• Subjects: Bacterial Proteins - biosynthesis; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Bacteriology; Biological and medical sciences; DegP protease; Escherichia coli; Escherichia coli - genetics; Escherichia coli - growth & development; Escherichia coli - metabolism; Fundamental and applied biological sciences. Psychology; Genes, Fungal; Genetics; Globomycin; Heat-Shock Proteins; Immunoblotting; Kinetics; Lipoprotein; Lipoproteins; Lysis protein; Magnesium - pharmacology; Microbiology; Mutation; Periplasmic Proteins; Plasmids; Serine Endopeptidases - metabolism; Species Specificity; Molecular processing; Enzyme; Proteolysis; Escherichia coli; Bacteria; Hydrolases; Proteinases; Structure function relationship; Enterobacteriaceae
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.1995.tb07354.x

The total amount of the colicin A lysis protein produced by cells grown in rich medium was analysed by immunoblotting. The intermediate forms of synthesis of this small lipoprotein were present in the cells at any time of induction, confirming that processing and maturation of colicin A lysis protein are slow and incomplete processes. The level of these various forms varied according to the time of induction, the growth conditions, the producing strain and the plasmid carrying the cal gene. It depended mainly on the presence in the producing strain of a degP gene which encodes the DegP protease. According to growth conditions, the DegP protease hydrolysed either a part or the total amount of the acylated precursor form. In some cases, a protease(s) other than DegP seemed to act on either form(s) of the colicin A lysis protein.