A Cys-less variant of the bacterial ATP binding cassette protein MalK is functional in maltose transport and regulation |
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Authors: | Hunke S Schneider E |
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Affiliation: | Humboldt Universit?t zu Berlin, Institut für Biologie/Bakterienphysiologie, Germany. |
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Abstract: | The cysteine residues of the ABC protein MalK from Salmonella typhimurium maltose transport system (C40, C350, C360) were consecutively replaced by serines. Cys-less MalK was fully functional in maltose transport in vivo. Moreover, the activity of MalK as a repressor of other maltose-regulated genes was also retained. The absence of cysteine residues in the purified protein was verified by its failure to react with fluorescein-5-maleimide. In contrast to purified wild-type MalK, the ATPase activity of the C40S variant was insensitive to inhibition by N-ethylmaleimide. |
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