@Article{IPB-1702, author = {Bosch, M. and Wright, L. P. and Gershenzon, J. and Wasternack, C. and Hause, B. and Schaller, A. and Stintzi, A.}, title = {{Jasmonic acid and its precursor 12-oxophytodienoic acid control different aspects of constitutive and induced herbivore defenses in tomato}}, year = {2014}, pages = {396-410}, journal = {Plant Physiology}, doi = {10.1104/pp.114.237388}, url = {http://www.plantphysiol.org/search?author1=&fulltext=&pubdate_year=2014&volume=166&firstpage=396&submit=yes}, volume = {166}, abstract = {The jasmonate family of growth regulators includes the isoleucine conjugate of jasmonic acid (JA-Ile) and its biosynthetic precursor 12-oxophytodienoic acid (OPDA) as signaling molecules. In order to assess the relative contribution of JA/JA-Ile and OPDA to insect resistance in tomato, we silenced the expression of OPDA reductase (OPR3) by RNA interference. Consistent with a block in the biosynthetic pathway downstream of OPDA, OPR3-RNAi plants contained wild-type levels of OPDA but failed to accumulate JA or JA-Ile after wounding. JA/JA-Ile deficiency in OPR3-RNAi plants resulted in reduced trichome formation and impaired monoterpene and sesquiterpene production. The loss of these JA/JA-Ile-dependent defense traits rendered them more attractive to the specialist herbivore Manduca sexta with respect to feeding and oviposition. Oviposition preference resulted from reduced levels of repellant mono- and sesquiterpenes. Feeding preference, on the other hand, was caused by increased production of cis-3-hexenal acting as a feeding stimulant for M. sexta larvae in OPR3-RNAi plants. Despite impaired constitutive defenses and increased palatability of OPR3-RNAi leaves, larval development was indistinguishable on OPR3-RNAi and wild-type plants, and much delayed as compared to development on the JA/JA-Ile insensitive (jai1) mutant. Apparently, signaling through JAI1, the tomato ortholog of COI1 in Arabidopsis, is required for defense while the conversion of OPDA to JA/JA-Ile is not. Comparing the signaling activities of OPDA and JA/JA-Ile, we found that OPDA can substitute for JA/JA-Ile in the local induction of defense gene expression, but the production of JA/JA-Ile is required for a systemic response.} } @Article{IPB-1018, author = {Schilling, S. and Wasternack, C. and Demuth, H.U.}, title = {{Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution}}, year = {2008}, pages = {983-991}, journal = {Biol. Chem }, doi = {10.1515/BC.2008.111}, volume = {389}, } @Article{IPB-1295, author = {Colon-Carmona, A. and Chen, D.L. and Yeh, K.C. and Abel, S.}, title = {{Aux/IAA proteins are phosphorylated by phytochrome in vitro}}, year = {2000}, pages = {1728-1738}, journal = {Plant Physiology}, url = {http://www.plantphysiol.org/content/124/4/1728.abstract?sid=0f984af4-c856-4351-babb-929b34461f87}, volume = {124}, abstract = { Auxin/indole-3-acetic acid (Aux/IAA) genes encode short-lived transcription factors that are induced as a primary response to the plant growth hormone IAA or auxin. Gain-of-function mutations in Arabidopsis genes,SHY2/IAA3, AXR3/IAA17, andAXR2/IAA7 cause pleiotropic phenotypes consistent with enhanced auxin responses, possibly by increasing Aux/IAA protein stability. Semidominant mutations shy2-1D,shy2-2, axr3-1, and axr2-1induce ectopic light responses in dark-grown seedlings. Because genetic studies suggest that the shy2-1D andshy2-2 mutations bypass phytochrome requirement for certain aspects of photomorphogenesis, we tested whether SHY2/IAA3 and related Aux/IAA proteins interact directly with phytochrome and whether they are substrates for its protein kinase activity. Here we show that recombinant Aux/IAA proteins from Arabidopsis and pea (Pisum sativum) interact in vitro with recombinant phytochrome A from oat (Avena sativa). We further show that recombinant SHY2/IAA3, AXR3/IAA17, IAA1, IAA9, and Ps-IAA4 are phosphorylated by recombinant oat phytochrome A in vitro. Deletion analysis of Ps-IAA4 indicates that phytochrome A phosphorylation occurs on the N-terminal half of the protein. Metabolic labeling and immunoprecipitation studies with affinity-purified antibodies to IAA3 demonstrate increased in vivo steady-state levels of mutant IAA3 in shy2-2 plants and phosphorylation of the SHY2-2 protein in vivo. Phytochrome-dependent phosphorylation of Aux/IAA proteins is proposed to provide one molecular mechanism for integrating auxin and light signaling in plant development.} }