Genetic and enzymatic basis of hygromycin B resistance in Escherichia coli
Author(s) -
R.Nagaraja Rao,
Norris E. Allen,
J N Hobbs,
William E. Alborn,
Herbert A. Kirst,
Jonathan W. Paschal
Publication year - 1983
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.24.5.689
Subject(s) - hygromycin b , escherichia coli , aminocyclitol , plasmid , phosphotransferase , biology , neomycin , microbiology and biotechnology , gene , aminoglycoside , biochemistry , antibiotics
A plasmid conferring resistance to the aminocyclitol antibiotic hygromycin B was isolated from Escherichia coli. The gene conferring resistance to this drug was cloned in pBR322, and the gene was localized to a fragment of ca. 1,510 base pairs. Resistance to hygromycin B is determined by an aminocyclitol phosphotransferase that modifies hygromycin B and structurally related antibiotics. The specific modification of hygromycin B is a phosphorylation of the hydroxyl on the 4 position of the cyclitol ring (hyosamine). The presence of the phosphotransferase in E. coli correlates with reduced accumulation of [14C]hygromycin B.
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