Subcellular localization and in vivo oxidation-reduction kinetics of thiol peroxidase in Escherichia coli.
Peroxiredoxins are a class of peroxide-scavenging enzymes having a conserved cysteine residue(s) in their active centers. Thiol peroxidase (Tpx) is one of the peroxiredoxins identified in Escherichia coli. Despite the absence of the N-terminal signal sequence for transport across the membrane, it has been characterized as a periplasmic protein. Reanalysis of Tpx localization, using active site cysteine mutants of thioredoxin 1 (Trx1), demonstrated that Tpx forms a mixed-disulfide complex with cytoplasmic Trx1, indicating that Tpx localizes in the cytoplasm.
Tao
Kazuyuki
K
Radioisotope Center, University of Tokyo, Bunkyo-ku, Tokyo, Japan. tao@ric.u-tokyo.ac.jp
D002458:Cell Fractionation / Q000379:methods*; D003593:Cytoplasm / Q000201:enzymology*; D048168:Escherichia coli K12 / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D006861:Hydrogen Peroxide; D007700:Kinetics; D009154:Mutation; D009997:Osmotic Pressure; D010084:Oxidation-Reduction; D033903:Periplasmic Proteins / Q000235:genetics / Q000378:metabolism*; D010544:Peroxidases / Q000235:genetics / Q000378:metabolism*; D010957:Plasmids / Q000235:genetics; D013104:Spheroplasts; D013879:Thioredoxins / Q000235:genetics / Q000378:metabolism
D029968:Escherichia coli Proteins; D033903:Periplasmic Proteins; D013879:Thioredoxins; D006861:Hydrogen Peroxide; D010544:Peroxidases; C097049:Tpx protein, E coli