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Plant and Cell Physiology Advance Access published online on August 8, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci182
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Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received March 3, 2005
Accepted July 26, 2005

Regular Paper

Analysis of the Transport Activity of Barley Sucrose Transporter HvSUT1

Alicia B. Sivitz 1, Anke Reinders 1, and John M. Ward 1*

1 Department of Plant Biology, University of Minnesota Twin Cities, 1445 Gortner Ave., 250 Biological Sciences Center, St. Paul, MN 55108 USA

* To whom correspondence should be addressed.
John M. Ward, E-mail: jward{at}tc.umn.edu


  Abstract

Localization studies indicate that barley (Hordeum vulgare) sucrose transporter HvSUT1 functions in sucrose uptake into seeds during grain filling. To further understand the physiological function of HvSUT1, we have expressed the HvSUT1 cDNA in Xenopus laevis oocytes and analyzed the transport activity by two-electrode voltage clamping. Consistent with a H+-coupled transport mechanism, sucrose induced large inward currents in HvSUT1-expressing oocytes with a K0.5 of 3.8 mM at pH 5.0 and a membrane potential of -157 mV. Of 21 other sugars tested, four glucosides were also transported by HvSUT1. These glucosides were maltose, salicin (2-(hydroxymethyl) phenyl {beta}-D-glucoside), {alpha}-phenylglucoside and {alpha}-paranitrophenylglucoside. Kinetic analysis of transport of these substrates by HvSUT1 was performed and K0.5 values were measured. The apparent affinity for all substrates was dependent on membrane potential and pH with lower K0.5 values at lower external pH and more negative membrane potentials. HvSUT1 was more selective for {alpha}-glucosides over {beta}-glucosides than the Arabidopsis sucrose transporter AtSUC2. Several substrates transported by AtSUC2 ({beta}-phenyl glucoside, {beta}-paranitrophenyl glucoside, {alpha}-methyl glucoside, turanose, and arbutin (hydroquinone {beta}-D glucoside)) showed low or undetectable transport by HvSUT1. Of these, {beta}-paranitrophenyl glucoside inhibited sucrose transport by HvSUT1 indicating that it interacts with the transporter while arbutin and {alpha}-methyl glucoside did not inhibit. The results demonstrate significant differences in substrate specificity between HvSUT1 and AtSUC2.

Keywords: Hordeum vulgare; sucrose transporter; HvSUT1; oocyte expression; electrophysiology.
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