Identification of a plastidial phenylalanine exporter that influences flux distribution through the phenylalanine biosynthetic network
In addition to proteins, L -phenylalanine is a versatile precursor for thousands of plant metabolites. Production of phenylalanine-derived compounds is a complex multi-compartmental process using phenylalanine synthesized predominantly in plastids as precursor. The transporter(s) exporting phenylala...
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Published in | Nature communications Vol. 6; no. 1; p. 8142 |
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Main Authors | , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group UK
10.09.2015
Nature Publishing Group Nature Pub. Group |
Subjects | |
Online Access | Get full text |
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Summary: | In addition to proteins,
L
-phenylalanine is a versatile precursor for thousands of plant metabolites. Production of phenylalanine-derived compounds is a complex multi-compartmental process using phenylalanine synthesized predominantly in plastids as precursor. The transporter(s) exporting phenylalanine from plastids, however, remains unknown. Here, a gene encoding a
Petunia hybrida
plastidial cationic amino-acid transporter (PhpCAT) functioning in plastidial phenylalanine export is identified based on homology to an
Escherichia coli
phenylalanine transporter and co-expression with phenylalanine metabolic genes. Radiolabel transport assays show that PhpCAT exports all three aromatic amino acids.
PhpCAT
downregulation and overexpression result in decreased and increased levels, respectively, of phenylalanine-derived volatiles, as well as phenylalanine, tyrosine and their biosynthetic intermediates. Metabolic flux analysis reveals that flux through the plastidial phenylalanine biosynthetic pathway is reduced in
PhpCAT
RNAi lines, suggesting that the rate of phenylalanine export from plastids contributes to regulating flux through the aromatic amino-acid network.
Phenylalanine is synthesized in plant chloroplasts and is then exported to the cytosol, where it is a precursor for various secondary metabolites. Here, the authors identify PhpCAT as a plastid phenylalanine transporter required to maintain metabolic flux in petunia. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 USDOE Office of Science (SC), Biological and Environmental Research (BER) Gordon and Betty Moore Foundation (United States) SC0008628; GBMF2550.02 Present address: Indiana University School of Medicine South Bend, South Bend, Indiana 46617, USA Present address: Department of Biology, Duke University, Durham, North Carolina 27708, USA |
ISSN: | 2041-1723 2041-1723 |
DOI: | 10.1038/ncomms9142 |