Expression of Escherichia coli SecB in Bacillus subtilis facilitates secretion of the SecB-dependent maltose-binding protein of E. coli.

AUTOR(ES)

Collier, D N

RESUMO

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.

Documentos Relacionados

• Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli.
• prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli.
• Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli.
• The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.
• Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.