The DsbA-DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domains.
The DsbA and DsbB proteins of Escherichia coli are involved in facilitating the formation of disulfide bonds in periplasmic proteins. Here, we show that the rate of formation of a disulfide bond in the periplasmic domain of the inner membrane protein leader peptidase is reduced in dsbA and dsbB strains, whereas the rate of formation of a disulfide bond engineered into the membrane embedded domain of the same protein is completely unaffected by these mutations. We conclude that the Dsb proteins do not facilitate the formation of intramembraneous disulfides.
Whitley
P
P
Department of Molecular Biology, Karolinska Institute Center for Structural Biochemistry, NOVUM, Huddinge, Sweden.
von Heijne
G
G
D001426:Bacterial Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D007535:Isomerases / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases; D012697:Serine Endopeptidases
D001426:Bacterial Proteins; D004220:Disulfides; C079503:DsbB protein, Bacteria; D008565:Membrane Proteins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase; D007535:Isomerases; D019704:Protein Disulfide-Isomerases; D003545:Cysteine