First published online May 25, 2004; 10.1105/tpc.020297
The Plant Cell 16:1446-1465 (2004)
© 2004 American Society of Plant Biologists
Silencing of Hydroxycinnamoyl-Coenzyme A Shikimate/Quinate Hydroxycinnamoyltransferase Affects Phenylpropanoid Biosynthesis
Laurent Hoffmanna,
Sébastien Besseaua,
Pierrette Geoffroya,
Christophe Ritzenthalera,
Denise Meyera,
Catherine Lapierreb,
Brigitte Polletb and
Michel Legranda,1
a Institut de Biologie Moléculaire des Plantes, Unité Propre de Recherche, 2357 du Centre National de la Recherche Scientifique, Université Louis Pasteur, 67000 Strasbourg, France
b Laboratoire de Chimie Biologique, Unité Mixte de Recherche 206, Institut National de la Recherche Agronomique-Institut National Agronomique, 78850 Thiverval-Grignon, France
1 To whom correspondence should be addressed. E-mail michel.legrand{at}ibmp-ulp.u-strasbg.fr; fax 33 388 614442.
The hydroxyl group in the 3-position of the phenylpropanoid compounds is introduced at the level of coumarate shikimate/quinate esters, whose synthesis implicates an acyltransferase activity. Specific antibodies raised against the recombinant tobacco (Nicotiana tabacum) acyltransferase revealed the accumulation of the enzyme in stem vascular tissues of tobacco, in accordance with a putative role in lignification. For functional analysis, the acyltransferase gene was silenced in Arabidopsis thaliana and N. benthamiana by RNA-mediated posttranscriptional gene silencing. In Arabidopsis, gene silencing resulted in a dwarf phenotype and changes in lignin composition as indicated by histochemical staining. An in-depth study of silenced N. benthamiana plants by immunological, histochemical, and chemical methods revealed the impact of acyltransferase silencing on soluble phenylpropanoids and lignin content and composition. In particular, a decrease in syringyl units and an increase in p-hydroxyphenyl units were recorded. Enzyme immunolocalization by confocal microscopy showed a correlation between enzyme accumulation levels and lignin composition in vascular cells. These results demonstrate the function of the acyltransferase in phenylpropanoid biosynthesis.
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