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Identification of a plastidial phenylalanine exporter that influences flux distribution through the phenylalanine biosynthetic network

Author

Listed:
  • Joshua R. Widhalm

    (Purdue University)

  • Michael Gutensohn

    (Purdue University)

  • Heejin Yoo

    (Purdue University
    Purdue University
    Present address: Department of Biology, Duke University, Durham, North Carolina 27708, USA)

  • Funmilayo Adebesin

    (Purdue University)

  • Yichun Qian

    (Purdue University
    Purdue University)

  • Longyun Guo

    (Purdue University)

  • Rohit Jaini

    (School of Chemical Engineering, Purdue University)

  • Joseph H. Lynch

    (Purdue University)

  • Rachel M. McCoy

    (Purdue University)

  • Jacob T. Shreve

    (Bioinformatics Core, Purdue University
    Present address: Indiana University School of Medicine South Bend, South Bend, Indiana 46617, USA)

  • Jyothi Thimmapuram

    (Bioinformatics Core, Purdue University)

  • David Rhodes

    (Purdue University)

  • John A. Morgan

    (Purdue University
    School of Chemical Engineering, Purdue University)

  • Natalia Dudareva

    (Purdue University
    Purdue University)

Abstract

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.

Suggested Citation

  • Joshua R. Widhalm & Michael Gutensohn & Heejin Yoo & Funmilayo Adebesin & Yichun Qian & Longyun Guo & Rohit Jaini & Joseph H. Lynch & Rachel M. McCoy & Jacob T. Shreve & Jyothi Thimmapuram & David Rho, 2015. "Identification of a plastidial phenylalanine exporter that influences flux distribution through the phenylalanine biosynthetic network," Nature Communications, Nature, vol. 6(1), pages 1-11, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9142
    DOI: 10.1038/ncomms9142
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    Cited by:

    1. Pan Liao & Itay Maoz & Meng-Ling Shih & Ji Hee Lee & Xing-Qi Huang & John A. Morgan & Natalia Dudareva, 2023. "Emission of floral volatiles is facilitated by cell-wall non-specific lipid transfer proteins," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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