Open AccessPhysical characterisation of the Escherichia coli B gene encoding nitroreductase and its over‐expression in Escherichia coli K12
Author(s) -
Michael N.P.,
Brehm J.K.,
Anlezark G.M.,
Minton N.P.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07284.x
Subject(s) - escherichia coli , nitroreductase , biology , enterobacteriaceae , gene , nucleic acid sequence , open reading frame , lac operon , peptide sequence , enterobacter cloacae , microbiology and biotechnology , biochemistry , genetics
The Escherichia coli B gene ( nfnB ) encoding nitroreductase has been cloned in Escherichia coli K‐12 and its nucleotide sequence determined. The translated amino acid sequence was found to share substantial identity (88.5%) with the equivalent proteins of Enterobacter cloacae and Salmonella typhimurium . When the structural gene was placed under the transcriptional control of either the trp or lac promoter, recombinant nitroreductase was accumulated to 33% and 25% of the cell's soluble protein, respectively. Substitution of the nfrB ribosome binding site with that of the E. coli lacZ gene reduced production levels of nitroreductase. The sequenced region also contained two incomplete open reading frames of unknown function.