A novel mutation in the alpha-helix 1 of the C subunit of the F(1)/F(0) ATPase responsible for optochin resistance of a Streptococcus pneumoniae clinical isolate.
Previously reported mutations involved in optochin resistance of Streptococcus pneumoniae clinical isolates changed residues 48, 49 or 50, in the transmembrane alpha-helix 2 of the F(1)/F(0) ATPase subunit. We report here an unusual mutation which changes the sequence of the transmembrane alpha-helix 1 of the AtpC subunit. This mutation involves a Gly to Ser substitution resulting from a G to A transition at codon 14 of the atpC gene.
Cogné
N
N
Laboratoire de Bactériologie-Virologie-Hygiène, CHU Dupuytren Unité CNRS-EP 118, 2 Avenue Martin Luther King 87042 Cedex, Limoges, France.
Claverys
J
J
Denis
F
F
Martin
C
C
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001483:Base Sequence; D004269:DNA, Bacterial; D004352:Drug Resistance, Microbial; D006801:Humans; D008969:Molecular Sequence Data; D016296:Mutagenesis; D006180:Proton-Translocating ATPases / Q000235:genetics*; D011803:Quinine / Q000031:analogs & derivatives* / Q000494:pharmacology; D013296:Streptococcus pneumoniae / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics / Q000302:isolation & purification
D000900:Anti-Bacterial Agents; D004269:DNA, Bacterial; C017303:ethylhydrocupreine; D011803:Quinine; D006180:Proton-Translocating ATPases