A 17 kDa outer-membrane protein (Omp4) from Serratia marcescens confers partial resistance to bacteriocin 28b when expressed in Escherichia coli

Article Abstract:

Escherichia coli transducted with DNA from Serratia marcescens N28b acquire partial insensitivity to bacteriocin 28b produced by Serratia. The insensitivity is due to the presence of Omp4, a 17kDa outer membrane protein encoded by the omp4 gene. Omp4 contains a terminal signal sequence and is similar in structure to the Enterobacteriaceae outer-membrane proteins. The omp4 gene contains an ORF, about 172 amino acids and its theoretical molecular mass is 18.4 kDa. Overexpression of omp4 decreases the amount of E. coli outer-membrane proteins OmpA, OmpF and OmpC.

Physiological aspects, Membrane proteins, Immunogenetics

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A novel protein of Erysipelothrix rhusiopathiae that confers haemolytic activity on Escherichia coli

Article Abstract:

A study was conducted to identify the gene encoding the haemolysin of Erysipelothrix rhusiopathiae and to compare the haemolysin to haemolysins in other pathogenic bacteria. Ery. rhusiopathiae Tama-96 was utilized as the basis for construction of a genomic library. Results indicated inverted repeat sequences inside the two direct repeat sequences. Findings also showed no sequence homology to the deduced amino acid sequence of ORF2.

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The NucE and NucD lysis proteins are not essential for secretion of the Serratia marcescens extracellular nuclease

Article Abstract:

A study was conducted to analyze the function of the NucE and NucD lysis proteins with respect to nuclease secretion in Serratia marcescens. DNA transformation was carried out by electroporation while DNA probes were labelled radioactively. Experimental results indicated that the genes promoted the extracellular secretion of nuclease from Escherichia coli when present on a multicopy plasmid.

Enzymes, Plasmids, Nucleases

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