Excretion of a protease by Serratia marcescens

Abstract

Excretion of an extracellular protease of Serratia marcescens ATCC 25419 occurred during logarithmic growth and was highest (per cell) when cultures reached the stationary growth phase. Production of the extracellular protease was induced by leucine or casein in minimal medium or by growth in tryptone-yeast medium. In the late stationary phase an intracellular protease activity accumulated which was also observed in mutants with very low extracellular protease activity. The excreted protease was the dominant protein in the growth medium. The protease was purified to homogeneity by column chromatography on Bio-Gel P-100 and on DEAE-cellulose. Quantitative amino acid analysis revealed the absence of sulfur-containing amino acids. The enzyme consists of one polypeptide chain. A molecular weiht of 51,000 and 55,000 was estimated using polyacrylamide gel electrophoresis and chromatography on Bio-Gel P-100 respectively. The enzyme cleaved only N-alpha-benzoyl-DL-lysine-and-arginine-nitroanilides but not the corresponding leucine or tyrosine derivatives nor a set of di- and tripeptides.

Cloning and expression in Escherichia coli of the Serratia marcescens metalloprotease gene: secretion of the protease from E. coli in the presence of the Erwinia chrysanthemi protease secretion functions

“…A common feature of many bacterial exoenzymes, including those from Serratia spp., is growth-phase-dependent expression (4,38). Little or no protein is synthesized in exponentially growing cells.…”

“…Serratia marcescens secretes a 50-kDa metalloprotease (SM protease) in large amounts into the culture medium (4). The gene encoding the exoprotease has been cloned and expressed in Escherichia coli, and its nucleotide sequence has been reported (32).…”

The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation

“…S. marcescens has been isolated from soil, water, plants and air (Grimont & Grimont, 1978). The ability of some S. marcescens strains to colonize a wide range of ecological niches has been linked to the production of a spectrum of extracellular products including chitinases, proteases, lipases, nucleases, bacteriocins, surfactants and wetting agents (Braun & Schmitz, 1980;Clegg & Allen, 1985;Hines et al, 1988;Matsuyama et al, 1995;Yanagida et al, 1986).…”

The Rap and Hor proteins of Erwinia, Serratia and Yersinia: a novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens

“…The ability of Sma to cause disease and to inhabit a wide variety of ecological niches has been linked to the production of an array of extracellular products, including proteases, chitinases, nucleases, lipases, wetting agents, bacteriocins and the bright red pigment, 2-methyl-3-pentyl-6-methoxyprodigiosin or prodigiosin (Pig; Braun and Schmitz, 1980;Clegg and Allen, 1985;Yanagida et al, 1986;Hines, 1988;Matsuyama et al, 1995).…”