Wound response characteristics as related to phenylpropanoid enzyme activity and lignin deposition in resistant and susceptible Populus tremuloides inoculated with Entoleuca mammata (Hypoxylon mammatum)

1998 ◽  
Vol 76 (7) ◽  
pp. 1282-1289 ◽  
Author(s):  
B Bucciarelli ◽  
H G Jung ◽  
M E Ostry ◽  
N A Anderson ◽  
C P Vance
Keyword(s):  
Alcohol Dehydrogenase ◽  
Caffeic Acid ◽  
Populus Tremuloides ◽  
Phenylalanine Ammonia Lyase ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Wound Response ◽  
Cinnamyl Alcohol ◽  
Susceptible Genotype ◽  
Zone Formation ◽  
Hypoxylon Mammatum

Green internodal stem tissues of glasshouse grown Populus tremuloides were either wounded or wound-inoculated with Entoleuca mammata (Hypoxylon mammatum) and assayed for phenylalanine ammonia-lyase (PAL), caffeic acid - o-methyltransferase (CA-OMT), and cinnamyl - alcohol dehydrogenase (CAD) activity over a 96-h period. Lignin deposited in response to the treatments was analyzed by the Klason and the pyrolysis - gas chromatographic (GC) - mass spectroscopy (MS) methodologies. The wound-inoculated treatment resulted in a wound morphology congruent with a typical resistant and susceptible response to E. mammata. Wounding alone resulted in no morphological differences between the two genotypes. In wound-inoculated stem tissue PAL and CAD activities were substantially higher in the resistant relative to the susceptible genotype. Total Klason lignin was similar for both genotypes; however, pyrolysis-GC-MS analysis revealed a difference in the lignin monomeric composition between the two genotypes, with the susceptible genotype accumulating higher levels of hydroxyphenyl units relative to the resistant genotype. It is concluded that differences in PAL and CAD activity and the synthesis of distinct phenylpropanoid monomers distinguish the resistant from the susceptible aspen genotype. Alterations in boundary zone formation due to the differential synthesis of phenylpropanoid monomers and its effect on compartmentalization of the pathogen are discussed.Key words: aspen, Hypoxylon canker, phenylalanine ammonia-lyase, cinnamyl - alcohol dehydrogenase, caffeic acid - o-methyltransferase, disease resistance.

scholarly journals Functional characterization of cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase in Brachypodium distachyon

2013 ◽  
Vol 13 (1) ◽  
pp. 61 ◽  
Author(s):  
Gina M Trabucco ◽  
Dominick A Matos ◽  
Scott J Lee ◽  
Aaron J Saathoff ◽  
Henry D Priest ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Caffeic Acid ◽  
Brachypodium Distachyon ◽  
Functional Characterization ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol

scholarly journals Differential Effects of Phenylalanine Ammonia Lyase, Cinnamyl Alcohol Dehydrogenase, and Energetic Metabolism Inhibition on Resistance of Appropriate Host and Nonhost Cereal–Rust Interactions

2007 ◽  
Vol 97 (12) ◽  
pp. 1578-1583 ◽  
Author(s):  
E. Prats ◽  
F. Martínez ◽  
M. M. Rojas-Molina ◽  
D. Rubiales
Keyword(s):  
Powdery Mildew ◽  
Alcohol Dehydrogenase ◽  
Phenylalanine Ammonia Lyase ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Penetration Resistance ◽  
Host Cells ◽  
Cinnamyl Alcohol ◽  
Energetic Metabolism ◽  
Differential Effects ◽  
Metabolism Inhibition

Effects of phenylpropanoid and energetic metabolism inhibition on resistance were studied during appropriate host and nonhost cereal-rust interactions. In the appropriate barley–Puccinia hordei interaction, phenylalanine ammonia lyase (PAL) and cinnamyl alcohol dehydrogenase (CAD) inhibition reduced penetration resistance in two genotypes, suggesting a role for phenolics and lignins in resistance. Interestingly, penetration resistance of the barley genotype 17.5.16 was not affected by phenylpropanoid biosynthesis but penetration resistance was almost completely inhibited by D-mannose, which reduces the energy available in plant host cells. This suggests a parallel in the cellular basis of penetration resistance between 17.5.16 rust and mlo barleys powdery mildew interaction. Results revealed differing patterns of programmed cell death (PCD) in appropriate versus nonhost rust interactions. PAL and CAD inhibitors reduced PCD (hypersensitivity) in appropriate interactions. Conversely, they had no effect in PCD of wheat to P. hordei; whereas D-mannose dramatically reduced nonhost resistance and allowed colony establishment. The differential effects of inhibitors in the expression of the different resistances and the commonalities with the cereal-powdery mildew interaction is analyzed and discussed.

scholarly journals Sugarcane expressed sequences tags (ESTs) encoding enzymes involved in lignin biosynthesis pathways

2001 ◽  
Vol 24 (1-4) ◽  
pp. 235-241 ◽  
Author(s):  
Rose Lucia Braz Ramos ◽  
Francisco Javier Tovar ◽  
Ricardo Magrani Junqueira ◽  
Fabiane Borges Lino ◽  
Gilberto Sachetto-Martins
Keyword(s):  
Cell Wall ◽  
Alcohol Dehydrogenase ◽  
Caffeic Acid ◽  
Lignin Content ◽  
Lignin Biosynthesis ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol ◽  
Cinnamoyl Coa Reductase ◽  
Coa Reductase ◽  
Lignin Metabolism

Lignins are phenolic polymers found in the secondary wall of plant conductive systems where they play an important role by reducing the permeability of the cell wall to water. Lignins are also responsible for the rigidity of the cell wall and are involved in mechanisms of resistance to pathogens. The metabolic routes and enzymes involved in synthesis of lignins have been largely characterized and representative genes that encode enzymes involved in these processes have been cloned from several plant species. The synthesis of lignins is liked to the general metabolism of the phenylpropanoids in plants, having enzymes (e.g. phenylalanine ammonia-lyase (PAL), cinnamate 4-hydroxylase (C4H) and caffeic acid O-methyltransferase (COMT)) common to other processes as well as specific enzymes such as cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD). Some maize and sorghum mutants, shown to have defective in CAD and/or COMT activity, are easier to digest because they have a reduced lignin content, something which has motivated different research groups to alter the lignin content and composition of model plants by genetic engineering try to improve, for example, the efficiency of paper pulping and digestibility. In the work reported in this paper, we have made an inventory of the sugarcane expressed sequence tag (EST) coding for enzymes involved in lignin metabolism which are present in the sugarcane EST genome project (SUCEST) database. Our analysis focused on the key enzymes ferulate-5-hydroxylase (F5H), caffeic acid O-methyltransferase (COMT), caffeoyl CoA O-methyltransferase (CCoAOMT), hydroxycinnamate CoA ligase (4CL), cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD). The comparative analysis of these genes with those described in other species could be used as molecular markers for breeding as well as for the manipulation of lignin metabolism in sugarcane.

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