Expression of Escherichia coli SecB in Bacillus subtilis facilitates secretion of the SecB-dependent maltose-binding protein of E. coli.
Less than 20% of the Escherichia coli maltose-binding protein (MBP) synthesized in Bacillus subtilis is exported. However, a portion of the secreted MBP was processed cotranslationally. Coexpression of SecB, a secretion-related chaperone of E. coli, stimulated posttranslational export of MBP in B. subtilis but inhibited its cotranslational processing. Export of a SecB-independent MBP-ribose-binding protein hybrid precursor was not enhanced by SecB. A slowly folding MBP derivative (MBP-Y283D) was more efficiently secreted than wild-type MBP, suggesting that the antifolding activity of SecB promotes posttranslational secretion of MBP in B. subtilis.
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Central Research and Development Division, E. I. DuPont de Nemours & Co., Wilmington, Delaware 19880-0328.
D018528:ATP-Binding Cassette Transporters; D001412:Bacillus subtilis / Q000235:genetics*; D001426:Bacterial Proteins / Q000502:physiology*; D001483:Base Sequence; D002352:Carrier Proteins / Q000378:metabolism*; D018833:Chaperonins; D017931:DNA Primers / Q000737:chemistry; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D058619:Maltose-Binding Proteins; D008969:Molecular Sequence Data; D009004:Monosaccharide Transport Proteins; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002352:Carrier Proteins; D017931:DNA Primers; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D011506:Proteins; D012333:RNA, Messenger; C057842:SecB protein, Bacteria; C461599:maltose transport system, E coli; D018833:Chaperonins