title: Abscisic acid and jasmonic acid activate wound-inducible genes in potato through separate, organ-specific signal transduction pathways.
abstract: Mechanical damage to leaf tissue causes an increase in abscisic acid (ABA) which in turn activates the biosynthesis of jasmonic acid (JA). The resulting higher endogenous JA levels subsequently activate the expression of wound-inducible genes. This study shows that JA induces the expression of different sets of genes in roots and leaves of potato plants. When roots of intact plants were treated with JA, high levels of proteinase inhibitor II (pin2), cathepsin D inhibitor, leucine aminopeptidase and threonine deaminase mRNAs accumulated in the systemic leaves. However, in the treated roots, very low, if any, expression of these genes could be detected. In contrast, a novel, root-specific pin2 homologue accumulated in the JA-treated root tissue which could not be detected in leaves, either systemic or those directly treated with JA. Application of okadaic acid and staurosporine revealed that a protein phosphorylation step is involved in the regulation of this differential response. In leaves, a protein phosphatase is required for the JA-induced expression of pin2 and the other genes analysed. This phosphatase activity is not necessary for the JA-induced expression of a pin2 homologue in roots, suggesting the existence of different transduction pathways for the JA signal in these organs. The requirement of a protein phosphatase activity for JA-mediated gene induction has enabled identification of a JA-independent pathway for ABA induction of pin2 and the other wound-inducible genes. This alternative pathway involves a protein kinase, and appears to be selective for wound-inducible genes. Our data suggest the presence of a complex, organ-specific transduction network for regulating the effects of the plant hormones ABA and JA on gene expression upon wounding.
authors.affiliation: Centro Nacional de Biotecnología CSIC, Madrid, Spain.
authors.forename: C
authors.initials: C
authors.lastname: Dammann
authors.forename: E
authors.initials: E
authors.lastname: Rojo
authors.forename: J J
authors.initials: JJ
authors.lastname: Sánchez-Serrano
mesh_terms: D000040:Abscisic Acid / Q000494:pharmacology*; D000595:Amino Acid Sequence; D002402:Cathepsin D / Q000037:antagonists & inhibitors; D003517:Cyclopentanes / Q000494:pharmacology*; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D017343:Genes, Plant / Q000187:drug effects*; D007931:Leucyl Aminopeptidase / Q000235:genetics; D008969:Molecular Sequence Data; D009928:Organ Specificity; D054883:Oxylipins; D010940:Plant Proteins / Q000235:genetics; D011480:Protease Inhibitors / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D018749:RNA, Plant / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction / Q000187:drug effects / Q000235:genetics; D011198:Solanum tuberosum / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism; D013913:Threonine Dehydratase / Q000235:genetics; D015533:Transcriptional Activation
chemical_list: D003517:Cyclopentanes; D054883:Oxylipins; D010940:Plant Proteins; D011480:Protease Inhibitors; D012333:RNA, Messenger; D018749:RNA, Plant; C034104:proteinase inhibitor II protein, plant; C011006:jasmonic acid; D000040:Abscisic Acid; D007931:Leucyl Aminopeptidase; D002402:Cathepsin D; D013913:Threonine Dehydratase