First published online October 3, 2002; 10.1104/pp.006262
Plant Physiol, October 2002, Vol. 130, pp. 796-807
Differential Expression of Two Distinct Phenylalanine
Ammonia-Lyase Genes in Condensed Tannin-Accumulating and Lignifying
Cells of Quaking Aspen
Yu-Ying
Kao,
Scott A.
Harding, and
Chung-Jui
Tsai*
Plant Biotechnology Research Center, School of Forestry and Wood
Products, Michigan Technological University, Houghton, Michigan
49931
Lignins, along with condensed tannins (CTs) and salicylate-derived
phenolic glycosides, constitute potentially large phenylpropanoid carbon sinks in tissues of quaking aspen (Populus
tremuloides Michx.). Metabolic commitment to each of these
sinks varies during development and adaptation, and depends on
L-phenylalanine ammonia-lyase (PAL), an enzyme catalyzing
the deamination of L-phenylalanine to initiate
phenylpropanoid metabolism. In Populus spp., PAL is encoded by multiple genes whose expression has been associated with
lignification in primary and secondary tissues. We now report cloning
two differentially expressed PAL cDNAs that exhibit
distinct spatial associations with CT and lignin biosynthesis in
developing shoot and root tissues of aspen. PtPAL1 was
expressed in certain CT-accumulating, non-lignifying cells of stems,
leaves, and roots, and the pattern of PtPAL1 expression
varied coordinately with that of CT accumulation along the primary to
secondary growth transition in stems. PtPAL2 was
expressed in heavily lignified structural cells of shoots, but was also
expressed in non-lignifying cells of root tips. Evidence of a role for
Pt4CL2, encoding 4-coumarate:coenzyme A ligase, in
determining CT sink strength was gained from cellular co-expression
analysis with PAL1 and CTs, and from experiments in
which leaf wounding increased PAL1 and
4CL2 expression as well as the relative allocation of
carbon to CT with respect to phenolic glycoside, the dominant phenolic
sink in aspen leaves. Leaf wounding also increased PAL2
and lignin pathway gene expression, but to a smaller extent. The
absence of PAL2 in most CT-accumulating cells provides
in situ support for the idea that PAL isoforms function in specific
metabolic milieus.
*
Corresponding author; e-mail chtsai{at}mtu.edu; fax
906-487-2915.
© 2002 American Society of Plant Physiologists
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