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Nucleotide sequence and structural relationships of a chloramphenicol acetyltransferase encoded by the plasmid pSCS6 from Staphylococcus aureus
Author(s) -
Cardoso Marisa,
Schwarz S.
Publication year - 1992
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1992.tb01837.x
Subject(s) - chloramphenicol acetyltransferase , plasmid , biology , staphylococcus aureus , peptide sequence , gene , nucleic acid sequence , open reading frame , acetyltransferase , chloramphenicol , amino acid , genetics , microbiology and biotechnology , bacteria , promoter , acetylation , gene expression
M. CARDOSO AND S. SCHWARZ. 1992. The 4.6 kb chloramphenicol resistance (Cm R ) plasmid, pSCS6, isolated from a naturally occurring Staphylococcus aureus biotype C encoded an inducible chloramphenicol acetyltransferase (CAT). The respective cat gene and its regulatory region were cloned. Sequence analyses revealed two open reading frames: one for a 9‐amino acid leader peptide and the other for the 215‐amino acid CAT monomer. Comparisons of the predicted CAT amino acid sequences revealed a high degree of similarity between CAT from pSCS6 and the CAT variants encoded by Cm R plasmids of the pC221 family. These close structural relationships suggested an intraspecific exchange of Cm R ‐determinants between Staph. aureus of human and bovine biotype.