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Journal of Bacteriology, August 2001, p. 4900-4904, Vol. 183, No. 16
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.16.4900-4904.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Specificity and Topology of the Escherichia coli Xanthosine Permease, a Representative of the NHS Subfamily of the Major Facilitator Superfamily

Morten H. H. Nørholm and Gert Dandanell*

Department of Biological Chemistry, Institute of Molecular Biology, University of Copenhagen, 1307 Copenhagen K, Denmark

Received 5 March 2001/Accepted 24 May 2001

The specificity of XapB permease was compared with that of the known nucleoside transporters NupG and NupC. XapB-mediated xanthosine uptake is abolished by 2,4-dinitrophenol and exhibits saturation kinetics with an apparent Km of 136 µM. A 12-transmembrane-segment model was confirmed by translational fusions to alkaline phosphatase and the alpha  fragment of beta -galactosidase.

* Corresponding author. Mailing address: Department of Biological Chemistry, University of Copenhagen, Sølvgade 83 H, 1307 Copenhagen K, Denmark. Phone: 45 35 32 20 25. Fax: 45 35 32 20 40. E-mail: dandanell{at}mermaid.molbio.ku.dk.

Journal of Bacteriology, August 2001, p. 4900-4904, Vol. 183, No. 16
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.16.4900-4904.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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