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Completion of the cytosolic post-chorismate phenylalanine biosynthetic pathway in plants.
Nat Commun 2019; 10(1):15NC

Abstract

In addition to being a vital component of proteins, phenylalanine is also a precursor of numerous aromatic primary and secondary metabolites with broad physiological functions. In plants phenylalanine is synthesized predominantly via the arogenate pathway in plastids. Here, we describe the structure, molecular players and subcellular localization of a microbial-like phenylpyruvate pathway for phenylalanine biosynthesis in plants. Using a reverse genetic approach and metabolic flux analysis, we provide evidence that the cytosolic chorismate mutase is responsible for directing carbon flux towards cytosolic phenylalanine production via the phenylpyruvate pathway. We also show that an alternative transcription start site of a known plastidial enzyme produces a functional cytosolic prephenate dehydratase that catalyzes the conversion of prephenate to phenylpyruvate, the intermediate step between chorismate mutase and phenylpyruvate aminotransferase. Thus, our results complete elucidation of phenylalanine biosynthesis via phenylpyruvate in plants, showing that this pathway splits from the known plastidial arogenate pathway at chorismate, instead of prephenate as previously thought, and the complete pathway is localized in the cytosol.

Authors+Show Affiliations

Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr., West Lafayette, IN, 47907-2010, USA.Department of Biochemistry, Purdue University, 175 South University St., West Lafayette, IN, 47907-2063, USA.Department of Biochemistry, Purdue University, 175 South University St., West Lafayette, IN, 47907-2063, USA.Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr., West Lafayette, IN, 47907-2010, USA.Department of Biochemistry, Purdue University, 175 South University St., West Lafayette, IN, 47907-2063, USA. Davidson School of Chemical Engineering, Purdue University, 480 Stadium Mall Dr., West Lafayette, IN, 47907-2100, USA.Department of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr., West Lafayette, IN, 47907-2010, USA. dudareva@purdue.edu. Department of Biochemistry, Purdue University, 175 South University St., West Lafayette, IN, 47907-2063, USA. dudareva@purdue.edu. Purdue Center for Plant Biology, Purdue University, West Lafayette, IN, 47907, USA. dudareva@purdue.edu.

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

30604768

Citation

Qian, Yichun, et al. "Completion of the Cytosolic Post-chorismate Phenylalanine Biosynthetic Pathway in Plants." Nature Communications, vol. 10, no. 1, 2019, p. 15.
Qian Y, Lynch JH, Guo L, et al. Completion of the cytosolic post-chorismate phenylalanine biosynthetic pathway in plants. Nat Commun. 2019;10(1):15.
Qian, Y., Lynch, J. H., Guo, L., Rhodes, D., Morgan, J. A., & Dudareva, N. (2019). Completion of the cytosolic post-chorismate phenylalanine biosynthetic pathway in plants. Nature Communications, 10(1), p. 15. doi:10.1038/s41467-018-07969-2.
Qian Y, et al. Completion of the Cytosolic Post-chorismate Phenylalanine Biosynthetic Pathway in Plants. Nat Commun. 2019 01 3;10(1):15. PubMed PMID: 30604768.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Completion of the cytosolic post-chorismate phenylalanine biosynthetic pathway in plants. AU - Qian,Yichun, AU - Lynch,Joseph H, AU - Guo,Longyun, AU - Rhodes,David, AU - Morgan,John A, AU - Dudareva,Natalia, Y1 - 2019/01/03/ PY - 2018/06/26/received PY - 2018/12/05/accepted PY - 2019/1/4/entrez PY - 2019/1/4/pubmed PY - 2019/3/21/medline SP - 15 EP - 15 JF - Nature communications JO - Nat Commun VL - 10 IS - 1 N2 - In addition to being a vital component of proteins, phenylalanine is also a precursor of numerous aromatic primary and secondary metabolites with broad physiological functions. In plants phenylalanine is synthesized predominantly via the arogenate pathway in plastids. Here, we describe the structure, molecular players and subcellular localization of a microbial-like phenylpyruvate pathway for phenylalanine biosynthesis in plants. Using a reverse genetic approach and metabolic flux analysis, we provide evidence that the cytosolic chorismate mutase is responsible for directing carbon flux towards cytosolic phenylalanine production via the phenylpyruvate pathway. We also show that an alternative transcription start site of a known plastidial enzyme produces a functional cytosolic prephenate dehydratase that catalyzes the conversion of prephenate to phenylpyruvate, the intermediate step between chorismate mutase and phenylpyruvate aminotransferase. Thus, our results complete elucidation of phenylalanine biosynthesis via phenylpyruvate in plants, showing that this pathway splits from the known plastidial arogenate pathway at chorismate, instead of prephenate as previously thought, and the complete pathway is localized in the cytosol. SN - 2041-1723 UR - https://www.unboundmedicine.com/medline/citation/30604768/Completion_of_the_cytosolic_post-chorismate_phenylalanine_biosynthetic_pathway_in_plants L2 - http://dx.doi.org/10.1038/s41467-018-07969-2 DB - PRIME DP - Unbound Medicine ER -