Disulfide bond formation in secreton component PulK provides a possible explanation for the role of DsbA in pullulanase secretion

Results show that the Klebsiella oxytoca cells defective in secretion of pullulanase, because of a mutation in the gene encoding a periplasmic disulfide oxidoreductase pullulanase, are rectified by the overproduction of pseudopilin PulK. Data indicate that pseudopilin contains reduced disulfide bonds, which impair the secretion process.