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Two components of the Yersinia enterocolitica maltose transport system, maltoporin (OmpM) and an osmotically shockable periplasmic maltose-binding protein (MBP) were identified. The synthesis of OmpM (apparent M r 43000) and transport of maltose into cells of Y. enterocolitica were induced by maltose and maltodextrins. A mutant lacking OmpM was drastically impaired in maltose transport, independent of induction by maltose. The MBP of Y. enterocolitica (apparent M r 40000) was found in the osmotic shock fluid. Its synthesis was induced by maltose. Moreover, rabbit antibodies raised against the MBP of E. coli cross-reacted with the analogous protein from Y. enterocolitica. The MBP of Y. enterocolitica restored the maltose transport activities in ΔmalE mutant cells of E. coli.
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