title: Silencing ribulose-1,5-bisphosphate carboxylase/oxygenase expression does not disrupt nitrogen allocation to defense after simulated herbivory in Nicotiana attenuata.
abstract: Ribulose-1,5-bisphosphate carboxylase/ oxygenase (RuBisCO) is the most abundant protein on the planet and in addition to its central role in photosynthesis it is thought to function as a nitrogen (N)-storage protein and a potential source of N for defense biosynthesis in plants. In a recent study in the wild tobacco Nicotiana attenuata, we showed that the decrease in absolute N invested in soluble proteins and RuBisCO elicited by simulated herbivory was much larger than the N-requirements of nicotine and phenolamide biosynthesis; (15)N flux studies revealed that N for defensive phenolamide synthesis originates from recently assimilated N rather than from RuBisCO turnover. Here we show that a transgenic line of N. attenuata silenced in the expression of RuBisCO (asRUB) invests similar or even larger amounts of N into phenolamide biosynthesis compared with wild type plants, consistent with our previous conclusion that recently assimilated N is channeled into phenolamide synthesis after elicitation. We suggest that the decrease in leaf proteins after simulated herbivory is a tolerance mechanism, rather than a consequence of N-demand for defense biosynthesis.
authors.affiliation: Department of Molecular Ecology; Max Planck Institute for Chemical Ecology; Jena, Germany.
authors.forename: Mariana A
authors.initials: MA
authors.lastname: Stanton
authors.affiliation: Department of Molecular Ecology; Max Planck Institute for Chemical Ecology; Jena, Germany; Qiagen; Hilden, Germany.
authors.forename: Lynn
authors.initials: L
authors.lastname: Ullmann-Zeunert
authors.affiliation: MS Group; Max Planck Institute for Chemical Ecology; Jena, Germany.
authors.forename: Natalie
authors.initials: N
authors.lastname: Wielsch
authors.affiliation: Department of Bioorganic Chemistry; Max Planck Institute for Chemical Ecology; Jena, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Bartram
authors.affiliation: MS Group; Max Planck Institute for Chemical Ecology; Jena, Germany.
authors.forename: Aleš
authors.initials: A
authors.lastname: Svatoš
authors.affiliation: Department of Molecular Ecology; Max Planck Institute for Chemical Ecology; Jena, Germany.
authors.forename: Ian T
authors.initials: IT
authors.lastname: Baldwin
authors.affiliation: Department of Molecular Ecology; Max Planck Institute for Chemical Ecology; Jena, Germany.
authors.forename: Karin
authors.initials: K
authors.lastname: Groten
mesh_terms: D000818:Animals; D020868:Gene Silencing; D060434:Herbivory / Q000502:physiology*; D018402:Manduca / Q000502:physiology*; D008954:Models, Biological; D009538:Nicotine / Q000378:metabolism; D009584:Nitrogen / Q000378:metabolism*; D009587:Nitrogen Isotopes; D021122:Protein Subunits / Q000378:metabolism; D011700:Putrescine / Q000378:metabolism; D012273:Ribulose-Bisphosphate Carboxylase / Q000235:genetics* / Q000378:metabolism; D013095:Spermidine / Q000378:metabolism; D014026:Nicotiana / Q000201:enzymology* / Q000276:immunology*
chemical_list: D009587:Nitrogen Isotopes; D021122:Protein Subunits; D009538:Nicotine; D012273:Ribulose-Bisphosphate Carboxylase; D009584:Nitrogen; D013095:Spermidine; D011700:Putrescine
keywords: caffeoyl-putrescine; dicaffeoyl-spermidine; growth-defense trade-off; ribulose-1,5-bisphosphate carboxylase/ oxygenase; total soluble protein