Wounding induces the first enzyme of the shikimate pathway in Solanaceae

The first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (EC 4.1.2.15), is induced by wounding potato or tomato tissue. The increase in enzyme activity is associated with elevated amounts of the enzyme as determined by immunoblots. The specific wound-induced pr...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 86; no. 19; pp. 7370 - 7373
Main Authors Dyer, W.E. (Purdue University, West Lafayette, IN), Henstrand, J.M, Handa, A.K, Herrmann, K.M
Format Journal Article
LanguageEnglish
Published Washington, DC National Academy of Sciences of the United States of America 01.10.1989
National Acad Sciences
Subjects
AMONIO FENILALANINA LIASA
Antibodies
ARN MENSAJERO
ARN MESSAGER
Biological and medical sciences
Biological Sciences: Biochemistry
Enzyme activity
Enzymes
EXPRESION GENICA
EXPRESSION DES GENES
FEUILLE
Fundamental and applied biological sciences. Psychology
Gels
GENETICA
GENETIQUE
HOJAS
LIASAS
Lignin
LYASE
LYCOPERSICON ESCULENTUM
Messenger RNA
Metabolism
PHENYLALANINE AMMONIA LYASE
phospho-2-dehydro-3-deoxyheptonate aldolase
Plant physiology and development
RNA
Shikimate pathway
shikimic acid
Sodium
SOLANUM TUBEROSUM
TALLO
TIGE
TUBERCULE
TUBERCULO
Tubers
Vegetals
Messenger RNA
In vitro translation
Enzymatic activity
Enzyme
Phospho-2-keto«-3-»deoxy-heptonate aldolase
Biosynthesis
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Summary:The first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (EC 4.1.2.15), is induced by wounding potato or tomato tissue. The increase in enzyme activity is associated with elevated amounts of the enzyme as determined by immunoblots. The specific wound-induced protein synthesis is preceded by an increase in the mRNA encoding this enzyme. The induced mRNA of potato tuber, leaf, and stem tissue is translated into a precursor polypeptide that is recognized by antibodies raised against the mature enzyme from tuber plastids. Wounding also induces mRNA encoding phenylalanine ammonia-lyase (EC 4.3.1.5), a key enzyme of plant secondary metabolism. The time courses for the induction of the two enzymes are similar, suggesting coordinate regulation for the biosynthesis of primary and secondary aromatic compounds
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ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.86.19.7370