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THE PLANT CELL, Vol 9, Issue 11 1985-1998, Copyright © 1997 by American Society of Plant Biologists
Antisense Suppression of 4-Coumarate:Coenzyme A Ligase Activity in Arabidopsis Leads to Altered Lignin Subunit Composition
D. Lee, K. Meyer, C. Chapple and C. J. Douglas
Department of Botany, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada
The phenylpropanoid enzyme 4-coumarate:coenzyme A ligase (4CL) is
considered necessary to activate the hydroxycinnamic acids for the
biosynthesis of the coniferyl and sinapyl alcohols subsequently polymerized
into lignin. To clarify the role played by 4CL in the biosynthesis of the
guaiacyl (G) and syringyl (S) units characteristic of angiosperm lignin, we
generated 4CL antisense Arabidopsis lines having as low as 8% residual 4CL
activity. The plants had decreases in thioglycolic acid-extractable lignin
correlating with decreases in 4CL activity. Nitrobenzene oxidation of cell
walls from bolting stems revealed a significant decrease in G units in
4CL-suppressed plants; however, levels of S lignin units were unchanged in
even the most severely 4CL-suppressed plants. These effects led to a large
decrease in the G/S ratio in these plants. Our results suggest that an
uncharacterized metabolic route to sinapyl alcohol, which is independent of
4CL, may exist in Arabidopsis. They also demonstrate that repression of 4CL
activity may provide an avenue to manipulate angiosperm lignin subunit
composition in a predictable manner.
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