Open AccessConstruction of chromosomally encoded secreted hemolysin fusion proteins by use of mini‐Tn hly A s transposon
Author(s) -
Spreng S,
Gentschev I
Publication year - 1998
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.1574-6968.1998.tb13145.x
Subject(s) - hemolysin , biology , secretion , escherichia coli , vtec , gene , signal peptide , fusion protein , microbiology and biotechnology , biochemistry , genetics , peptide sequence , virulence , recombinant dna
We used the minitransposon Tn hlyA s [Gentschev, I., Maier, G., Kranig, A. and Goebel, W. (1996) Mol. Gen. Genet. 252, 266–274] for random insertion of the secretion signal (HlyA s ) of Escherichia coli hemolysin (HlyA) into chromosomal genes. Four mini‐Tn hlyA s derivatives bearing the gltA (citrate synthase), deoC (2 deoxyribose‐5 phosphate aldolase), tig (trigger factor) genes and an unknown ORF fused to hlyA s were identified and characterized. Our data suggest that Tn hlyA s ‐generated hemolysin fusion proteins are secreted efficiently by the HlyB/HlyD/TolC hemolysin secretion machinery and that this can be useful for studies of gene expression or function.