Differential expression of two distinct phenylalanine ammonia-lyase genes in condensed tannin-accumulating and lignifying cells of quaking aspen.
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.
Kao
Yu-Ying
YY
Plant Biotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton, MI 49931, USA.
Harding
Scott A
SA
Tsai
Chung-Jui
CJ
D029681:Arabidopsis Proteins; D015152:Blotting, Northern; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D003624:Darkness; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D047348:Hydrolyzable Tannins / Q000378:metabolism*; D017403:In Situ Hybridization; D008031:Lignin / Q000378:metabolism*; D008969:Molecular Sequence Data; D010636:Phenols / Q000378:metabolism; D010650:Phenylalanine Ammonia-Lyase / Q000235:genetics / Q000378:metabolism*; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D032107:Populus / Q000166:cytology / Q000201:enzymology* / Q000235:genetics; D020156:Salicylic Acid / Q000494:pharmacology; D017422:Sequence Analysis, DNA; D012697:Serine Endopeptidases; D013314:Stress, Mechanical
D029681:Arabidopsis Proteins; D018076:DNA, Complementary; D047348:Hydrolyzable Tannins; D010636:Phenols; D010940:Plant Proteins; D008031:Lignin; D012697:Serine Endopeptidases; D010650:Phenylalanine Ammonia-Lyase; D020156:Salicylic Acid