First published online April 9, 2002; 10.1104/pp.010988
Plant Physiol, May 2002, Vol. 129, pp. 145-155
Laccase Down-Regulation Causes Alterations in Phenolic Metabolism
and Cell Wall Structure in Poplar1
Philippe
Ranocha,
Matthieu
Chabannes,
Simon
Chamayou,
Saïda
Danoun,
Alain
Jauneau,
Alain-M.
Boudet, and
Deborah
Goffner*
Unité Mixte de Recherche, Centre National de la
Recherche Scientifique-Université Paul Sabatier 5546 "Signaux
et Messages Cellulaires chez les Végétaux," Pôle de
Biotechnologie Végétale, 24, Chemin de Borde Rouge, 31326 Castanet Tolosan, France
Laccases are encoded by multigene families in plants.
Previously, we reported the cloning and characterization of five
divergent laccase genes from poplar (Populus
trichocarpa) xylem. To investigate the role of individual
laccase genes in plant development, and more particularly in
lignification, three independent populations of antisense poplar
plants, lac3AS, lac90AS, and
lac110AS with significantly reduced levels of laccase
expression were generated. A repression of laccase gene expression had
no effect on overall growth and development. Moreover, neither lignin
content nor composition was significantly altered as a result of
laccase suppression. However, one of the transgenic populations,
lac3AS, exhibited a 2- to 3-fold increase in total
soluble phenolic content. As indicated by toluidine blue staining,
these phenolics preferentially accumulate in xylem ray parenchyma
cells. In addition, light and electron microscopic observations of
lac3AS stems indicated that lac3 gene
suppression led to a dramatic alteration of xylem fiber cell walls.
Individual fiber cells were severely deformed, exhibiting modifications
in fluorescence emission at the primary wall/middle lamella region and
frequent sites of cell wall detachment. Although a direct correlation
between laccase gene expression and lignification could not be
assigned, we show that the gene product of lac3 is essential for normal cell wall structure and integrity in xylem fibers.
lac3AS plants provide a unique opportunity to explore laccase function in plants.
1
This work was supported by the European
Commission (Agro-Industrial Research program, grant no.
AIR2-CT93-1661), by the Centre National de la Recherche
Scientifique, by the Université Paul Sabatier, and by the
Ministère de l'Enseignement Supérieur et de la Recherche
(fellowship to P.R.).
*
Corresponding author; e-mail goffner{at}smcv.ups-tlse.fr; fax
33-562-19-35-02.
© 2002 American Society of Plant Physiologists
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