The contribution of electrostatic forces to the process of adherence of Candida albicans yeast cells to substrates |
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Authors: | Stephen A Klotz |
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Institution: | Thermophile and Microbial Biochemistry and Biotechnology Unit, University of Waikato, Private Bag 3105, Hamilton, New Zealand; Section of Microbiology, Cornell University, Ithaca, NY 14853, USA; Agricultural Research Service, USDA, Ithaca, NY 14853, USA |
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Abstract: | Abstract Thermoanaerobacter thermohydrosulfuricus Rt8.B1 catabolized xylose by the pentose phosphate pathway, and xylose isomerase and xylulokinase were inducible. The uptake of xylose was by two low-affinity, inducible systems. Both systems were resistant to the protonophore, tetrachlorosalicylanilide, the F1F0-ATPase inhibitor, N , N -dicyclohexylcarboiimide, and the sodium/proton antiporter, monensin. The high capacity system (100 nmol min−1 (mg protein)−1) was only expressed when the bacterium was grown with a high concentration of xylose (50 mM). It took more than 60 mM xylose to saturate the high capacity system. When T. thermohydrosulfuricus was grown with a low concentration of xylose (5 mM), xylose uptake was saturated by as little as 10 mM xylose (18 nmol min−1 (mg protein)−1). Cells grown with 50 mM xylose could not transport glucose, and high capacity xylose transport was not inhibited by glucose or non-metabolizable glucose analogues. Cells grown with 5 mM xylose transported glucose at a rapid rate (30 nmol min−1 (mg protein)−1), and low capacity xylose uptake was competitively inhibited by either glucose or 2-deoxy-glucose. Because the glucose uptake of cells grown on 5 mM xylose was competitively inhibited by xylose, it appeared that the low capacity xylose uptake system was a glucose/xylose carrier. |
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Keywords: | Xylose uptake Low affinity Thermoanaerobacter thermohydrosulfuricus Thermophile |
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