Glucose Transport in the Extremely Thermoacidophilic Sulfolobus solfataricus Involves a High-Affinity Membrane-Integrated Binding Protein

Author:

Albers Sonja-V.1,Elferink Marieke G. L.1,Charlebois Robert L.2,Sensen Christoph W.3,Driessen Arnold J. M.1,Konings Wil N.1

Affiliation:

1. Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands,1 and

2. Department of Biology, University of Ottawa, Ottawa, Ontario K1N 6N5,2 and

3. Institute for Marine Biosciences, National Research Council of Canada, Halifax, Nova Scotia B3H 3Z1,3 Canada

Abstract

ABSTRACT The archaeon Sulfolobus solfataricus grows optimally at 80°C and pH 2.5 to 3.5 on carbon sources such as yeast extracts, tryptone, and various sugars. Cells rapidly accumulate glucose. This transport activity involves a membrane-bound glucose-binding protein that interacts with its substrate with very high affinity ( K d of 0.43 μM) and retains high glucose affinity at very low pH values (as low as pH 0.6). The binding protein was extracted with detergent and purified to homogeneity as a 65-kDa glycoprotein. The gene coding for the binding protein was identified in the S. solfataricus P2 genome by means of the amino-terminal amino acid sequence of the purified protein. Sequence analysis suggests that the protein is anchored to the membrane via an amino-terminal transmembrane segment. Neighboring genes encode two membrane proteins and an ATP-binding subunit that are transcribed in the reverse direction, whereas a homologous gene cluster in Pyrococcus horikoshii OT3 was found to be organized in an operon. These data indicate that S. solfataricus utilizes a binding-protein-dependent ATP-binding cassette transporter for the uptake of glucose.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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