Phenylalanine (Phe) biosynthesis in plants is a key process, as Phe serves as
precursor of proteins and phenylpropanoids. The prephenate pathway connects
chorismate, final product of the shikimate pathway, with the biosynthesis of Phe
and Tyr. Two alternative routes of Phe biosynthesis have been reported: one
depending of arogenate, and the other of phenylpyruvate. Whereas the arogenate
pathway is considered the main route, the role of the phenylpyruvate pathway
remains unclear. Here, we report that the deficiency in ADT2, a bifunctional
arogenate dehydratase (ADT)/ prephenate dehydratase (PDT) enzyme, causes
embryo arrest and seed abortion. This result makes a clear distinction between the
essential role of ADT2 and the five remaining ADTs from Arabidopsis, which
display mostly overlapping functions. We have found that PHA2, a monofunctional
PDT from yeast, restores the adt2 phenotype when is targeted within the plastids,
but not when is expressed in the cytosol. Similar results can be obtained by
expressing ADT3, a monofunctional ADT. These results suggest that Phe can be
synthesized from phenylpyruvate or arogenate when the bifunctional ADT2 is
replaced by other ADT or PDT enzymes during seed formation, highlighting the
importance of Phe for embryo development, and providing further insights into the
plasticity of Phe biosynthesis.Universidad de Málaga. Campus de Excelencia Internacional Andalucía Tech
