Phenylalanine ammonia-lyase from tomato cell cultures inoculated with Verticillium albo-atrum

Tomato (Lycopersicon esculentum Mill.) cell suspension cultures accumulated wall-bound phenolic materials in response to inoculation with Verticillium albo-atrum Reinke et Berth. in a fashion analogous to that observed in whole plants. Both monomeric and polymeric materials were recovered. Depositio...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1991-12, Vol.97 (4), p.1494-1500
Main Authors: Bernards, Mark A., Ellis, Brian E.
Format: Article
Language:English
Subjects:
actividad enzimatica
activite enzymatique
activity
Agronomy. Soil science and plant productions
amonio fenilalanina liasa
Biological and medical sciences
biosintesis
biosynthese
biosynthesis
cell culture
Cell culture techniques
cell suspensions
Cell walls
characterization
Chromatography
cultivo de celulas
culture de cellule
Cultured cells
Enzymes
enzymic activity
fitoalexina
Fundamental and applied biological sciences. Psychology
Fungal plant pathogens
Gels
host-pathogen interactions
Inoculation
Kinetics
Lycopersicon esculentum
metabolite
metabolites
metabolitos
pared celular
paroi cellulaire
Pathology, epidemiology, host-fungus relationships. Damages, economic importance
phenylalanine ammonia lyase
phytoalexine
phytoalexins
Phytopathology. Animal pests. Plant and forest protection
Plants
Protein isoforms
purificacion
purification
verticillium
Verticillium albo-atrum
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Description
Summary:Tomato (Lycopersicon esculentum Mill.) cell suspension cultures accumulated wall-bound phenolic materials in response to inoculation with Verticillium albo-atrum Reinke et Berth. in a fashion analogous to that observed in whole plants. Both monomeric and polymeric materials were recovered. Deposition of phenolics into the cell walls of inoculated tomato cell cultures was inhibited by the phenylalanine ammonia-tyase (PAL) inhibitor, 2-amino-2-indanephosphate. Tomato PAL activity was induced over 12-fold by fungal inoculation, with a concomitant increase in the corresponding mRNA. The enzyme was purified >3400-fold, to apparent homogeneity, by anion-exchange chromatography, chromatofocusing, and gel filtration. The holoenzyme had a molecular mass of 280 to 320 kilodaltons, comprising 74-kilodalton subunits, and displayed an isoelectric point of 5.6 to 5.7. Induced PAL displayed apparent Michaelis-Menten kinetics (Km = 116 micromolar) and was not appreciably inhibited by its product cinnamic acid. Chromatographic analysis did not reveal multiple forms of the enzyme in either inoculated or uninoculated cultures.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.97.4.1494