MATE2 Mediates Vacuolar Sequestration of Flavonoid Glycosides and Glycoside Malonates in Medicago truncatula Metadata
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- Main Title MATE2 Mediates Vacuolar Sequestration of Flavonoid Glycosides and Glycoside Malonates in Medicago truncatula
Author: Zhao, JianCreator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Huhman, DavidCreator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Shadle, Gail L.Creator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: He, Xian-ZhiCreator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Sumner, Lloyd W.Creator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Tang, YuhongCreator Type: PersonalCreator Info: Samuel Roberts Noble Foundation
Author: Dixon, R. A.Creator Type: PersonalCreator Info: University of North Texas; Samuel Roberts Noble Foundation
Name: Association Society of Plant BiologistsPlace of Publication: [Rockville, Maryland]
- Creation: 2011-04
- Content Description: Article on MATE2 mediating vacuolar sequestration of flavonoid glycosides and glycoside malonates in Medicago truncatula.
- Physical Description: 21 p.
- Keyword: MATE2
- Keyword: Medicago truncatula
- Keyword: biosynthesis
- Journal: The Plant Cell, 2011, Rockville: American Society of Plant Biologists, pp. 1536-1555
- Publication Title: The Plant Cell
- Volume: 23
- Issue: 4
- Page Start: 1536
- Page End: 1555
- Peer Reviewed: True
Name: UNT Scholarly WorksCode: UNTSW
Name: UNT College of Arts and SciencesCode: UNTCAS
- Rights Access: public
- DOI: 10.1105/tpc.110.080804
- Archival Resource Key: ark:/67531/metadc282595
- Academic Department: Biological Sciences
- Display Note: Abstract: The majority of flavonoids, such as anthocyanins, proanthocyanidins, and isoflavones, are stored in the central vacuole, but the molecular basis of flavonoid transport is still poorly understood. Here, we report the functional characterization of a multidrug and toxin extrusion transporter (MATE2), from Medicago truncatula. MATE 2 is expressed primarily in leaves and flowers. Despite its high similarity to the epicatechin 3′-O-glucoside transporter MATE1, MATE2 cannot efficiently transport proanthocyanidin precursors. In contrast, MATE2 shows higher transport capacity for anthocyanins and lower efficiency for other flavonoid glycosides. Three malonyltransferases that are coexpressed with MATE2 were identified. The malonylated flavonoid glucosides generated by these malonyltransferases are more efficiently taken up into MATE2-containing membrane vesicles than are the parent glycosides. Malonylation increases both the affinity and transport efficiency of flavonoid glucosides for uptake by MATE2. Genetic loss of MATE2 function leads to the disappearance of leaf anthocyanin pigmentation and pale flower color as a result of drastic decreases in the levels of various flavonoids. However, some flavonoid glycoside malonates accumulate to higher levels in MATE2 knockouts than in wild-type controls. Deletion of MATE2 increases seed proanthocyanidin biosynthesis, presumably via redirection of metabolic flux from anthocyanin storage.
- Display Note: Copyright © 2011 American Society of Plant Biologists. The following article appeared in The Plant Cell, 23:4, pp. 1536-1555, http://www.plantcell.org/content/23/4/1536.long