Maltose uptake and its regulation in Bacillus subtilis

M. Tangney, C. J. Buchanan, F. G. Priest, W. J. Mitchell

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    25 Citations (Scopus)


    Extracts prepared from cultures of Bacillus subtilis, grown on maltose as the sole carbon source, lacked maltose phosphotransferase system activity. There was, however, evidence for a maltose phosphorylase activity, and such extracts also possessed both glucokinase and glucose phosphotransferase system activities. Maltose was accumulated by whole cells of B. subtilis by an energy-dependent mechanism. This uptake was sensitive to the effects of uncouplers, suggesting a role for the proton-motive force in maltose transport. Accumulation of maltose was inhibited in the presence of glucose, and there was no accumulation of maltose by a strain carrying the ptsI6 null-mutation. A strain carrying the temperature-sensitive ptsI1 mutation accumulated maltose normally at 37°C but, in contrast to the wild-type, was devoid of maltose transport activity at 47°C. The results indicate a role for the phosphotransferase system in the regulation of maltose transport activity in this organism.

    Original languageEnglish
    Pages (from-to)191-196
    Number of pages6
    JournalFEMS Microbiology Letters
    Issue number1-2
    Publication statusPublished - 1992


    • Bacillus subtilis
    • maltose uptake
    • phosphotransferase system


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