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Related Experiment Videos

Substrate recognition by a sucrose transporting protein.

W D Hitz, P J Card, K G Ripp

    The Journal of Biological Chemistry
    |September 15, 1986
    PubMed
    Summary

    Soybean cotyledon protoplasts reveal how sucrose transporters recognize their substrate. Hydrophobic interactions and specific hydroxyl groups on sucrose are key for binding to the carrier protein active site.

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    Plant physiology·1994

    Area of Science:

    • Plant biochemistry
    • Membrane transport
    • Molecular interactions

    Background:

    • Sucrose is a vital carbohydrate in plants, requiring specific transporters for cellular uptake.
    • Understanding sucrose transporter substrate recognition is crucial for optimizing plant physiology and crop yield.

    Purpose of the Study:

    • To investigate the molecular basis of substrate recognition by a soybean sucrose transporter.
    • To identify key structural features of sucrose involved in binding to the transporter.

    Main Methods:

    • Utilized protoplasts from developing soybean cotyledons.
    • Employed competitive inhibition assays with radiolabeled sucrose ([14C] sucrose) and various sucrose derivatives.
    • Analyzed binding interactions using phenyl-alpha-D-glucopyranoside and phenyl-alpha-D-thioglucopyranoside analogs.

    Main Results:

    • Five fructosyl-substituted sucrose derivatives, phenyl-alpha-D-glucopyranoside, and phenyl-alpha-D-thioglucopyranoside effectively inhibited [14C] sucrose influx.
    • Evidence suggests a significant role for hydrophobic interactions between the sucrose molecule and the transporter's binding site.
    • Modifications of glucosyl hydroxyls at positions 3, 4, and 6 on phenyl-alpha-D-thioglucopyranoside indicated their involvement in carrier recognition.

    Conclusions:

    • Soybean sucrose transporter recognition involves both hydrophobic interactions and specific hydroxyl group contacts.
    • The binding site accommodates a hydrophobic moiety of the substrate, likely contributing significantly to affinity.
    • Specific hydroxyl groups (at positions 3, 4, and 6) are critical for precise substrate recognition by the sucrose carrier protein.

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