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THE PLANT CELL, Vol 2, Issue 9 837-848, Copyright © 1990 by American Society of Plant Biologists
Functional Properties of a Phenylalanine Ammonia-Lyase Promoter from Arabidopsis
S. Ohl, S. A. Hedrick, J. Chory and C. J. Lamb
Plant Biology Laboratory, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037
Phenylalanine ammonia-lyase (PAL) is encoded by a small family of genes in
Arabidopsis. We cloned and partially characterized one of these genes,
PAL1. The deduced amino acid sequence is highly similar to PAL from bean,
parsley, and rice. The promoter contains sequence elements homologous to
two putative regulatory elements conserved among several phenylpropanoid
genes. The regulation of the PAL1 gene was examined by analysis of
[beta]-glucuronidase (GUS) activity in transgenic Arabidopsis containing
PAL1-GUS gene fusions. The PAL1 promoter was activated early in seedling
development and in adult plants was strongly expressed in the vascular
tissues of roots and leaves, but was not active in the root tip or the
shoot apical meristem. In flowers, expression was observed in sepals,
anthers, and carpels, but not in petals. Transcripts encoded by the
endogenous PAL genes and GUS transcripts from the PAL1-GUS gene fusion were
induced by wounding, HgCl2-stress, and light. Analysis of the regulatory
properties of 5[prime] deleted promoters showed that the proximal region of
the promoter to -290 was sufficient to establish the full tissue-specific
pattern of expression and that the proximal region to -540 was responsive
to environmental stimuli. Negative and positive elements were located
between -1816 and -823 and between -823 and -290, respectively.
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