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First published online June 3, 2005; 10.1105/tpc.105.030767

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The Plant Cell 17:2059-2076 (2005)
© 2005 American Society of Plant Biologists

CINNAMYL ALCOHOL DEHYDROGENASE-C and -D Are the Primary Genes Involved in Lignin Biosynthesis in the Floral Stem of Arabidopsis{boxw}

Richard Sibouta, Aymerick Eudesb, Gregory Mouilleb, Brigitte Polletc, Catherine Lapierrec, Lise Jouaninb and Armand Séguina,1

a Natural Resources Canada, Canadian Forest Service, Laurentian Forestry Centre, Sainte-Foy, QC G1V 4C7, Canada
b Institut National de la Recherche Agronomique, Département de Biologie Cellulaire, Institut Jean-Pierre Bourgin, 78026 Versailles Cedex, France
c Institut National de la Recherche Agronomique–Institut National d'Agronomie de Paris-Grignon, Département de Chimie Biologique, 78850 Thiverval-Grignon, France

1 To whom correspondence should be addressed. E-mail armand.seguin{at}nrcan.gc.ca; fax 418-648-5849.

During lignin biosynthesis in angiosperms, coniferyl and sinapyl aldehydes are believed to be converted into their corresponding alcohols by cinnamyl alcohol dehydrogenase (CAD) and by sinapyl alcohol dehydrogenase (SAD), respectively. This work clearly shows that CAD-C and CAD-D act as the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis thaliana by supplying both coniferyl and sinapyl alcohols. An Arabidopsis CAD double mutant (cad-c cad-d) resulted in a phenotype with a limp floral stem at maturity as well as modifications in the pattern of lignin staining. Lignin content of the mutant stem was reduced by 40%, with a 94% reduction, relative to the wild type, in conventional ß-O-4–linked guaiacyl and syringyl units and incorportion of coniferyl and sinapyl aldehydes. Fourier transform infrared spectroscopy demonstrated that both xylem vessels and fibers were affected. GeneChip data and real-time PCR analysis revealed that transcription of CAD homologs and other genes mainly involved in cell wall integrity were also altered in the double mutant. In addition, molecular complementation of the double mutant by tissue-specific expression of CAD derived from various species suggests different abilities of these genes/proteins to produce syringyl-lignin moieties but does not indicate a requirement for any specific SAD gene.




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