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Originally published In Press as doi:10.1074/jbc.M308490200 on September 3, 2003
J. Biol. Chem., Vol. 278, Issue 45, 44320-44325, November 7, 2003
Substrate Specificity of the Arabidopsis thaliana Sucrose Transporter AtSUC2*
Divya Chandran,
Anke Reinders, and
John M. Ward
From the
Department of Plant Biology, University of Minnesota Twin Cities, St. Paul, Minnesota 55108
The Arabidopsis sucrose transporter AtSUC2 is expressed in the companion cells of the phloem (specialized vascular tissue) and is essential for the long distance transport of carbohydrates within the plant. A variety of glucosides are known to inhibit sucrose uptake into yeast expressing AtSUC2; however, it remains unknown whether glucosides other than sucrose could serve as transported substrates. By expression of AtSUC2 in Xenopus oocytes and two-electrode voltage clamping, we have tested the ability of AtSUC2 to transport a range of physiological and synthetic glucosides. Sucrose induced inward currents with a K0.5 of 1.44 mM at pH 5 and a membrane potential of 137 mV. Of the 24 additional sugars tested, 8 glucosides induced large inward currents allowing kinetic analysis. These glucosides were maltose, arbutin (hydroquinone- -D-glucoside), salicin (2-(hydroxymethyl)phenyl- -D-glucoside), -phenylglucoside, -phenylglucoside, -paranitrophenylglucoside, -paranitrophenylglucoside, and paranitrophenyl- -thioglucoside. In addition, turanose and -methylglucoside induced small but significant inward currents indicating that they were transported by At-SUC2. The results indicate that AtSUC2 is not highly selective for -over -glucosides and may function in transporting glucosides besides sucrose into the phloem, and the results provide insight into the structural requirements for transport by AtSUC2.
Received for publication, August 2, 2003
, and in revised form, September 3, 2003.
* This work was supported by the United States Department of Energy Grant DE-FG02-03ER15414 (to J. M. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 612-625-4763; Fax: 612-625-1738; E-mail: jward{at}tc.umn.edu.

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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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