TY - JOUR ID - 701 TI - The wound response in tomato - Role of jasmonic acid JO - J. Plant Physiol PY - 2006 SP - 297-306 AU - Wasternack, C. AU - Stenzel, I. AU - Hause, B. AU - Hause, G. AU - Kutter, C. AU - Maucher, H. AU - Neumerkel, J. AU - Feussner, I. AU - Miersch, O. VL - 163 UR - DO - 10.1016/j.jplph.2005.10.014 AB - A2 - C1 - Molecular Signal Processing; Cell and Metabolic Biology ER - TY - JOUR ID - 388 TI - Induction of a new lipoxygenase form in cucumber leaves by salicylic acid or 2,6-dichloroisonicotinic acid JO - Bot. Acta PY - 1997 SP - 101-108 AU - Feussner, I. AU - Fritz, I.G. AU - Hause, B. AU - Ullrich, W.R. AU - Wasternack, C. VL - 110 UR - http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1438-8677/issues DO - 10.1111/j.1438-8677.1997.tb00616.x AB - Changes in lipoxygenase (LOX) protein pattern and/or activity were investigated in relation to acquired resistance of cucumber (Cucumis sativus L.) leaves against two powdery mildews, Sphaerotheca fuliginea (Schlecht) Salmon and Erysiphe cichoracearum DC et Merat. Acquired resistance was established by spraying leaves with salicylic acid (SA) or 2,6-dichloroisonicotinic acid (INA) and estimated in whole plants by infested leaf area compared to control plants. SA was more effective than INA. According to Western blots, untreated cucumber leaves contained a 97 kDa LOX form, which remained unchanged for up to 48 h after pathogen inoculation. Upon treatment with SA alone for 24 h or with INA plus pathogen, an additional 95 kDa LOX form appeared which had an isoelectric point in the alkaline range. For the induction of this form, a threshold concentration of 1 mM SA was required, higher SA concentrations did not change LOX-95 expression which remained similar between 24 h and 96 h but further increased upon mildew inoculation. Phloem exudates contained only the LOX-97 form, in intercellular washing fluid no LOX was detected. dichloroisonicotinic localization revealed LOX protein in the cytosol of the mesophyll cells without differences between the forms. A2 - C1 - Molecular Signal Processing; Cell and Metabolic Biology ER - TY - JOUR ID - 1301 TI - The PS-IAA4/5-like family of early auxin-inducible mRNAs in Arabidopsis thaliana JO - Journal of Biological Chemistry PY - 1995 SP - 19093-19099 AU - Abel, S. AU - Nguyen, M.D. AU - Theologis, A. VL - 270 UR - http://www.jbc.org/content/270/32/19093.abstract?sid=c17d6e17-db5e-4424-8236-1c3dccb9ded2 AB - 1-Aminocyclopropane-1-carboxylic acid (ACC) synthase is the key regulatory enzyme in the biosynthetic pathway of the plant hormone ethylene. The enzyme is encoded by a divergent multigene family in Arabidopsis thaliana, comprising at least five genes, ACS1-5 (Liang, X., Abel, S., Keller, J. A., Shen, N. F., and Theologis, A.(1992) Proc. Natl. Acad. Sci. U. S. A. 89, 11046-11050). In etiolated seedlings, ACS4 is specifically induced by indoleacetic acid (IAA). The response to IAA is rapid (within 25 min) and insensitive to protein synthesis inhibition, suggesting that the ACS4 gene expression is a primary response to IAA. The ACS4 mRNA accumulation displays a biphasic dose-response curve which is optimal at 10 μM of IAA. However, IAA concentrations as low as 100 nM are sufficient to enhance the basal level of ACS4 mRNA. The expression of ACS4 is defective in the Arabidopsis auxin-resistant mutant lines axr1-12, axr2-1, and aux1-7. ACS4 mRNA levels are severely reduced in axr1-12 and axr2-1 but are only 1.5-fold lower in aux1-7. IAA inducibility is abolished in axr2-1. The ACS4 gene was isolated and structurally characterized. The promoter contains four sequence motifs reminiscent of functionally defined auxin-responsive cis-elements in the early auxin-inducible genes PS-IAA4/5 from pea and GH3 from soybean. Conceptual translation of the coding region predicts a protein with a molecular mass of 53,795 Da and a theoretical isoelectric point of 8.2. The ACS4 polypeptide contains the 11 invariant amino acid residues conserved between aminotransferases and ACC synthases from various plant species. An ACS4 cDNA was generated by reverse transcriptase-polymerase chain reaction, and the authenticity was confirmed by expression of ACC synthase activity in Escherichia coli. A2 - C1 - Molecular Signal Processing ER -