Identification of a new gene responsible for the oxygen tolerance in aerobic life of Streptococcus mutans.
Alkyl hydroperoxide reductase in Streptococcus mutans consists of two components, Nox-1 and AhpC. Deletion of nox-1 and ahpC in a double mutant as well as the wild-type of Streptococcus mutans can form colonies in the presence of air to the same extent. The evidence suggested the presence of some other antioxidant system(s) independent of the Nox-1/AhpC system in the bacterium. Here we identified a new antioxidant gene (dpr) and the gene product (Dpr) which complements the defect of peroxidase activity caused by the deletion of nox-1 and ahpC in S. mutans. The dpr-disruption mutant of S. mutans could form colonies anaerobically but not aerobically.
Yamamoto
Y
Y
Department of Molecular and Cell Biology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Higuchi
M
M
Poole
L B
LB
Kamio
Y
Y
D000332:Aerobiosis / Q000235:genetics*; D000595:Amino Acid Sequence; D000975:Antioxidants / Q000378:metabolism*; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D015698:Genomic Library; D008969:Molecular Sequence Data; D009154:Mutation; D010545:Peroxides / Q000378:metabolism; D013295:Streptococcus mutans / Q000201:enzymology / Q000235:genetics*; D014170:Transformation, Genetic
D000975:Antioxidants; D002352:Carrier Proteins; D010545:Peroxides