SoxV, an orthologue of the CcdA disulfide transporter, is involved in thiosulfate oxidation in Rhodovulum sulfidophilum and reduces the periplasmic thioredoxin SoxW

• Published in: Biochemical and biophysical research communications 2002-08, Vol.296 (3), p.737-741
• Main Authors: Appia-Ayme, Corinne, Berks, Ben C
• Format: Article
• Language: English
• Subjects: Alphaproteobacteria - metabolism; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - physiology; Cell Membrane - metabolism; Disulfide; Disulfides - metabolism; DsbD; Electron transfer; Membrane Transport Proteins - genetics; Multigene Family; Oxidation-Reduction; Oxidoreductases - analysis; Photosynthesis; Sulfur bacteria; Thioredoxin-Disulfide Reductase - genetics; Thioredoxin-Disulfide Reductase - physiology; Thioredoxins - genetics; Thioredoxins - metabolism; Thiosulfate oxidation; Thiosulfates - metabolism
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(02)00936-1

Proteins of the CcdA/DsbD family have previously been found to be involved in the protein disulfide isomerase and cytochrome c maturation pathways of bacteria. SoxV is a CcdA homologue encoded by a genetic locus involved in lithotrophic thiosulfate oxidation in Rhodovulum sulfidophilum. Mutagenesis studies demonstrate an essential and specific role for SoxV in thiosulfate oxidation. Another protein encoded by the same locus, SoxW, is a periplasmic thioredoxin. SoxW was found to be in the reduced state during growth of R. sulfidophilum in the presence of thiosulfate. Maintenance of SoxW in the reduced state was shown to require SoxV. Nevertheless, SoxW was found to be dispensible for thiosulfate oxidation suggesting that SoxV reduces more than one periplasmic partner protein.