MATE2 Mediates Vacuolar Sequestration of Flavonoid Glycosides and Glycoside Malonates in Medicago truncatula

Description:

Article on MATE2 mediating vacuolar sequestration of flavonoid glycosides and glycoside malonates in Medicago truncatula.

Creator(s):
Creation Date: April 2011
Partner(s):
UNT College of Arts and Sciences
Collection(s):
UNT Scholarly Works
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Total Uses: 4
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Creator (Author):
Zhao, Jian

Samuel Roberts Noble Foundation

Creator (Author):
Huhman, David

Samuel Roberts Noble Foundation

Creator (Author):
Shadle, Gail

Samuel Roberts Noble Foundation

Creator (Author):
He, Xian-Zhi

Samuel Roberts Noble Foundation

Creator (Author):
Sumner, Lloyd W.

Samuel Roberts Noble Foundation

Creator (Author):
Tang, Yuhong

Samuel Roberts Noble Foundation

Creator (Author):
Dixon, R. A.

University of North Texas; Samuel Roberts Noble Foundation

Publisher Info:
Place of Publication: [Rockville, Maryland]
Date(s):
  • Creation: April 2011
Description:

Article on MATE2 mediating vacuolar sequestration of flavonoid glycosides and glycoside malonates in Medicago truncatula.

Degree:
Department: Biological Sciences
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.

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

Physical Description:

21 p.

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Subject(s):
Keyword(s): MATE2 | Medicago truncatula | biosynthesis
Source: The Plant Cell, 2011, Rockville: American Society of Plant Biologists, pp. 1536-1555
Partner:
UNT College of Arts and Sciences
Collection:
UNT Scholarly Works
Identifier:
  • DOI: 10.1105/tpc.110.080804
  • ARK: ark:/67531/metadc282595
Resource Type: Article
Format: Text
Rights:
Access: Public
Citation:
Publication Title: The Plant Cell
Volume: 23
Issue: 4
Page Start: 1536
Page End: 1555
Peer Reviewed: Yes