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Identification of a region of the enterobacterial OmpA protein used as a bacteriocin receptor
Author(s) -
Cole Stewart T.,
Maldener Marga
Publication year - 1986
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.1574-6968.1986.tb01226.x
Subject(s) - bacteriocin , shigella dysenteriae , colicin , escherichia coli , biology , shigella boydii , microbiology and biotechnology , gene , enterobacteriaceae , gene product , shigella , genetics , antimicrobial , gene expression
A hybrid gene has been constructed from the Escherichia coli and Shigella dysenteriae ompA genes. Its product differs from the E. coli OmpA protein only around amino acid 110. This substitution, resulting in the acquisition of a receptor site for bacteriocin 4–59 and loss of activity towards colicin L and phage K3, confirms the cell surface location of this region.

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