Probing binding specificity of the sucrose transporter AtSUC2 with fluorescent coumarin glucosides

The phloem sucrose transporter, AtSUC2, is promiscuous with respect to substrate recognition, transporting a range of glucosides in addition to sucrose, including naturally occurring coumarin glucosides. We used the inherent fluorescence of coumarin glucosides to probe the specificity of AtSUC2 for...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 69(2018), 10 vom: 27. Apr., Seite 2473-2482
1. Verfasser: De Moliner, Fabio (VerfasserIn)
Weitere Verfasser: Knox, Kirsten, Reinders, Anke, Ward, John M, McLaughlin, Paul J, Oparka, Karl, Vendrell, Marc
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Arabidopsis Proteins Coumarins Glucosides Membrane Transport Proteins Plant Proteins sucrose transport protein, plant coumarin A4VZ22K1WT
Beschreibung
Zusammenfassung:The phloem sucrose transporter, AtSUC2, is promiscuous with respect to substrate recognition, transporting a range of glucosides in addition to sucrose, including naturally occurring coumarin glucosides. We used the inherent fluorescence of coumarin glucosides to probe the specificity of AtSUC2 for its substrates, and determined the structure-activity relationships that confer phloem transport in vivo using Arabidopsis seedlings. In addition to natural coumarin glucosides, we synthesized new compounds to identify key structural features that specify recognition by AtSUC2. Our analysis of the structure-activity relationship revealed that the presence of a free hydroxyl group on the coumarin moiety is essential for binding by AtSUC2 and subsequent phloem mobility. Structural modeling of the AtSUC2 substrate-binding pocket explains some important structural requirements for the interaction of coumarin glucosides with the AtSUC2 transporter
Beschreibung:Date Completed 12.09.2019
Date Revised 12.09.2019
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/ery075