A pathway for disulfide bond formation in vivo.
Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations in the gene for a second protein, DsbB, which is also necessary for disulfide bond formation. Evidence suggests that DsbB may act by reoxidizing DsbA, thereby regenerating its ability to donate its disulfide bond to target proteins. We propose that DsbB, an integral membrane protein, may be involved in transducing redox potential across the cytoplasmic membrane.
Bardwell
J C
JC
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.
Lee
J O
JO
Jander
G
G
Martin
N
N
Belin
D
D
Beckwith
J
J
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D003553:Cystine / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005798:Genes, Bacterial; D007535:Isomerases / Q000235:genetics* / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D016296:Mutagenesis; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases; D011499:Protein Processing, Post-Translational
D001426:Bacterial Proteins; D004220:Disulfides; C079503:DsbB protein, Bacteria; D008565:Membrane Proteins; D003553:Cystine; D010088:Oxidoreductases; D007535:Isomerases; D019704:Protein Disulfide-Isomerases; D003545:Cysteine