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An ATP-binding cassette protein from grape berry (VvABCC1) transports glucosylated anthocyanins.
Type of publication
Peer-reviewed
Publikationsform
Original article (peer-reviewed)
Publication date
2013
Author
Francisco R, Regalado A, Agegeorges A, Burla B, Bassin B, Eisenach C, zarouk O, Chaves MM, Martinoia E, Nagy R,
Project
ABC transporters involved in signalling events
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Original article (peer-reviewed)
Journal
The Plant Cell
Volume (Issue)
25
Page(s)
1840 - 1854
Title of proceedings
The Plant Cell
DOI
doi/10.1105/tpc.112.102152
Open Access
URL
http://www.plantcell.org/content/25/5/1840.full.pdf#page=1&view=FitH
Type of Open Access
Publisher (Gold Open Access)
Abstract
Accumulation of anthocyanins in the exocarp of red grapevine (Vitis vinifera) cultivars is one of several events that characterize the onset of grape berry ripening (véraison). Despite our thorough understanding of anthocyanin biosynthesis and regulation, little is known about the molecular aspects of their transport. The participation of ATP binding cassette (ABC) proteins in vacuolar anthocyanin transport has long been a matter of debate. Here, we present biochemical evidence that an ABC protein, ABCC1, localizes to the tonoplast and is involved in the transport of glucosylated anthocyanidins. ABCC1 is expressed in the exocarp throughout berry development and ripening, with a significant increase at véraison (i.e., the onset of ripening). Transport experiments using microsomes isolated from ABCC1-expressing yeast cells showed that ABCC1 transports malvidin 3-O- glucoside. The transport strictly depends on the presence of GSH, which is cotransported with the anthocyanins and is sensitive to inhibitors of ABC proteins. By exposing anthocyanin-producing grapevine root cultures to buthionine sulphoximine, which reduced GSH levels, a decrease in anthocyanin concentration is observed. In conclusion, we provide evidence that ABCC1 acts as an anthocyanin transporter that depends on GSH without the formation of an anthocyanin-GSH conjugate.
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