期刊
PLANT JOURNAL
卷 63, 期 5, 页码 823-835出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1365-313X.2010.04287.x
关键词
phenylalanine; ADT; arogenate dehydratase; m-tyrosine; tryptophan; 2-phenylethylglucosinolate
资金
- Triad Foundation
- US National Science Foundation [MCB-0416567]
- Bi-national Agricultural Research and Development [US-3910-06]
P>A large proportion of plant carbon flow passes through the shikimate pathway to phenylalanine, which serves as a precursor for numerous secondary metabolites. To identify new regulatory mechanisms affecting phenylalanine metabolism, we isolated Arabidopsis thaliana mutants that are resistant to the phytotoxic amino acid m-tyrosine, a structural analog of phenylalanine. Map-based cloning identified adt2-1D, a dominant point mutation causing a predicted serine to alanine change in the regulatory domain of ADT2 (arogenate dehydratase 2). Relaxed feedback inhibition and increased expression of the mutant enzyme caused up to 160-fold higher accumulation of free phenylalanine in rosette leaves, as well as altered accumulation of several other primary and secondary metabolites. In particular, abundance of 2-phenylethylglucosinolate, which is normally almost undetectable in leaves of the A. thaliana Columbia-0 accession, is increased more than 30-fold. Other observed phenotypes of the adt2-1D mutant include abnormal leaf development, resistance to 5-methyltryptophan, reduced growth of the generalist lepidopteran herbivore Trichoplusia ni (cabbage looper) and increased salt tolerance.
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