Two genes encoding serine protease homologues in Serratia marcescens and characterization of their products in Escherichia coli

Journal of Biochemistry
Y OhnishiS Horinouchi

Abstract

A serine protease (SSP) of Serratia marcescens is one of the extracellular enzymes secreted from this Gram-negative bacterium. SSP is produced as a large precursor and converted to a mature protein by cleavages removing an NH2-terminal signal sequence and a COOH-terminal pro-region. This COOH-terminal pro-region is integrated into the outer membrane and has a functional role for the export of the mature protein across the outer membrane. Southern hybridization analysis with a DNA fragment encoding the COOH-terminal pro-region as the probe showed a wide distribution of nucleotide sequences encoding SSP exporter-like proteins among Serratia species. Moreover, S. marcescens IFO 3046, from which the ssp gene had been cloned, was found to contain two ssp homologues (ssp-h1 and ssp-h2). They were cloned and their nucleotide sequences were determined. The two ssp homologues were found to exist in tandem on the genome and their amino acid sequences showed 81% identity to each other. Both of them showed 55% identity in amino acid sequence to preproSSP. In addition, both showed end-to-end similarity to the 100 kDa serotype-specific antigen (Ssa1) of Pasteurella haemolytica. Escherichia coli JM105 containing ssp-h1 gene produced a 53 kDa ...Continue Reading

Citations

Jan 22, 2004·FEMS Microbiology Letters·Nick J ParhamIan R Henderson
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Apr 29, 2009·The Journal of Biological Chemistry·Marie-Ève CharbonneauMichael Mourez
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Dec 8, 2007·Microbiology and Molecular Biology Reviews : MMBR·Joachim Jose, Thomas F Meyer
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Jun 22, 2006·Microbial Cell Factories·Nancy Rutherford, Michael Mourez
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