A plasma membrane sucrose-binding protein that mediates sucrose uptake shares structural and sequence similarity with seed storage proteins but remains functionally distinct.

The Journal of Biological Chemistry
P J OvervoordeH D Grimes

Abstract

Photoaffinity labeling of a soybean cotyledon membrane fraction identified a sucrose-binding protein (SBP). Subsequent studies have shown that the SBP is a unique plasma membrane protein that mediates the linear uptake of sucrose in the presence of up to 30 mM external sucrose when ectopically expressed in yeast. Analysis of the SBP-deduced amino acid sequence indicates it lacks sequence similarity with other known transport proteins. Data presented here, however, indicate that the SBP shares significant sequence and structural homology with the vicilin-like seed storage proteins that organize into homotrimers. These similarities include a repeated sequence that forms the basis of the reiterated domain structure characteristic of the vicilin-like protein family. In addition, analytical ultracentrifugation and nonreducing SDS-polyacrylamide gel electrophoresis demonstrate that the SBP appears to be organized into oligomeric complexes with a Mr indicative of the existence of SBP homotrimers and homodimers. The structural similarity shared by the SBP and vicilin-like proteins provides a novel framework to explore the mechanistic basis of SBP-mediated sucrose uptake. Expression of the maize Glb protein (a vicilin-like protein close...Continue Reading

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Citations

Apr 12, 2000·European Journal of Biochemistry·J CastilloL Franco
May 22, 2007·Plant Physiology·Fatima AlkhalfiouiFrançoise Montrichard
Dec 1, 2004·Traffic·Dirk WenzelGiselbert Hinz
Feb 5, 2005·BMC Microbiology·Melanie HowellSheila A Hazlewood
Jan 10, 2006·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·Joseph BurdoDavid Schubert
Nov 3, 2005·Journal of Experimental Botany·Josefa CastilloM Isabel Rodrigo
Aug 12, 2000·Journal of Experimental Botany·J M Dunwell
Jul 28, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Nadia Al-SaediYonglin Ren

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