Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Published on January 9, 2009; 10.1104/pp.108.130070


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Received September 19, 2008
Accepted January 5, 2009

Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis

Pascal Rippert , Juliette Puyaubert , Delphine Grisolet , Laure Derrier , and Michel Matringe *

Laboratoire de Physiologie Cellulaire Vegetale, Institut National de la Recherche Agronomique, UMR 1200, 17 Rue des Martyrs F-38054 Grenoble, France; Laboratoire de Physiologie Cellulaire Vegetale, Centre de la Recherche Scientifique, UMR 5168, 17 Rue des Martyrs F-38054 Grenoble, France; Laboratoire de Physiologie Cellulaire Vegetale, Universite Grenoble I, 17 Rue des Martyrs F-38054 Grenoble, France; Laboratoire de Physiologie Cellulaire Vegetale, iRTSV Commissariat a l'Energie Atomique-Grenoble, 17 Rue des Martyrs F-38054 Grenoble, France;

* Corresponding author; email: michel.matringe{at}cea.fr.

While the presence of a complete shikimate pathway within plant plastids is definitively established, the existence of a cytosolic post-chorismate portion of the pathway is still debated. This question is alimented by the presence of a chorismate mutase within the cytosol. Until now, the only known destiny of prephenate, the product of chorismate mutase, is incorporation into tyrosine and/or phenylalanine. Therefore, the presence of a cytosolic chorismate mutase suggests that enzymes involved downstream chorismate mutase in tyrosine or phenylalanine biosynthesis could be present within the cytosol of plant cells. It was thus of particular interest to clarify the subcellular localization of arogenate dehydrogenases (TYRA) and arogenate dehydratases (ADT), which catalyze the ultimate steps in tyrosine and phenylalanine biosynthesis, respectively. The aim of the present study was to address this question in Arabidopsis by analysis the subcellular localization of the two TYRAAt and the six AtADT. The present work excludes the occurrence of a spliced TYRAAt1 transcript encoding a cytosolic TYRA protein. Transient expression analyses of TYRA- and ADT- GFP fusions reveal that the two Arabidopsis TYRA proteins and the six ADT proteins are all targeted within the plastid. Accordingly, TYRA and ADT proteins were both immunodetected in the chloroplast soluble protein fraction (stroma) of Arabidopsis. No TYRA or ADT proteins were immunodetected in the cytosol of Arabidopsis cells. Taken together, all our data exclude the possibility of tyrosine and/or phenylalanine synthesis within the cytosol, at least in green leaves and Arabidopsis cultured cells.




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