@article { ISI:000242621800023,
	title = {Molecular interactions between the specialist herbivore Manduca sexta (Lepidoptera, Sphingidae) and its natural host Nicotiana attenuata. VII. changes in the plant{\textquoteright}s proteome},
	journal = {Plant Physiology},
	volume = {142},
	number = {4},
	year = {2006},
	month = {DEC},
	pages = {1621-1641},
	publisher = {AMER SOC PLANT BIOLOGISTS},
	type = {Article},
	address = {15501 MONONA DRIVE, ROCKVILLE, MD 20855 USA},
	abstract = {<p>When Manduca sexta attacks Nicotiana attenuata, fatty acid-amino acid conjugates (FACs) in the larvae{\textquoteright}s oral secretions (OS) are introduced into feeding wounds. These FACs trigger a transcriptional response that is similar to the response induced by insect damage. Using two-dimensional gel electrophoresis, matrix-assisted laser desorption ionization-time of flight, and liquid chromatography-tandem mass spectrometry, we characterized the proteins in phenolic extracts and in a nuclear fraction of leaves elicited by larval attack, and/or in leaves wounded and treated with OS, FAC-free OS, and synthetic FACs. Phenolic extracts yielded approximately 600 protein spots, many of which were altered by elicitation, whereas nuclear protein fractions yielded approximately 100 spots, most of which were unchanged by elicitation. Reproducible elicitor-induced changes in 90 spots were characterized. In general, proteins that increased were involved in primary metabolism, defense, and transcriptional and translational regulation; those that decreased were involved in photosynthesis. Like the transcriptional defense responses, proteomic changes were strongly elicited by the FACs in OS. A semiquantitative reverse transcription-PCR approach based on peptide sequences was used to compare transcript and protein accumulation patterns for 17 candidate proteins. In six cases the patterns of elicited transcript accumulation were consistent with those of elicited protein accumulation. Functional analysis of one of the identified proteins involved in photosynthesis, RuBPCase activase, was accomplished by virus-induced gene silencing. Plants with decreased levels of RuBPCase activase protein had reduced photosynthetic rates and RuBPCase activity, and less biomass, responses consistent with those of herbivore-attacked plants. We conclude that the response of the plant{\textquoteright}s proteome to herbivore elicitation is complex, and integrated transcriptome-proteome-metabolome analysis is required to fully understand this ubiquitous ecological interaction.</p>},
	issn = {0032-0889},
	doi = {10.1104/pp.106.088781},
	author = {Giri, Ashok P. and Wuensche, Hendrik and Mitra, Sirsha Sribas and Zavala, Jorge A. and Muck, Alexander and Svatos, Ales and Baldwin, Ian T.}
}
@article { ISI:000298662500033,
	title = {MYB8 Controls inducible phenolamide levels by activating three novel hydroxycinnamoyl-coenzyme a:polyamine transferases in nicotiana attenuata},
	journal = {Plant Physiology},
	volume = {158},
	number = {1},
	year = {2012},
	month = {JAN},
	pages = {389-407},
	publisher = {AMER SOC PLANT BIOLOGISTS},
	address = {15501 MONONA DRIVE, ROCKVILLE, MD 20855 USA},
	abstract = {<p>A large number of plants accumulate N-acylated polyamines (phenolamides [PAs]) in response to biotic and/or abiotic stress conditions. In the native tobacco (Nicotiana attenuata), the accumulation of two major PAs, caffeoylputrescine and dicaffeoylspermidine (DCS), after herbivore attack is known to be controlled by a key transcription factor, MYB8. Using a broadly targeted metabolomics approach, we show that a much larger spectrum of PAs composed of hydroxycinnamic acids and two polyamines, putrescine and spermidine, is regulated by this transcription factor. We cloned several novel MYB8-regulated genes, annotated as putative acyltransferases, and analyzed their function. One of the novel acyltransferases (AT1) is shown to encode a hydroxycinnamoyl-coenzyme A: putrescine acyltransferase responsible for caffeoylputrescine biosynthesis in tobacco. Another gene (acyltransferase DH29), specific for spermidine conjugation, mediates the initial acylation step in DCS formation. Although this enzyme was not able to perform the second acylation toward DCS biosynthesis, another acyltransferase gene, CV86, proposed to act on monoacylated spermidines, was isolated and partially characterized. The activation of MYB8 in response to herbivore attack and associated signals required the activity of LIPOXYGENASE3, a gene involved in jasmonic acid (JA) biosynthesis in N. attenuata. These new results allow us to reconstruct a complete branch in JA signaling that defends N. attenuata plants against herbivores: JA via MYB8{\textquoteright}s transcriptional control of AT1 and DH29 genes controls the entire branch of PA biosynthesis, which allows N. attenuata to mount a chemically diverse (and likely efficient) defense shield against herbivores.</p>},
	issn = {0032-0889},
	doi = {10.1104/pp.111.187229},
	author = {Onkokesung, Nawaporn and Gaquerel, Emmanuel and Kotkar, Hemlata and Kaur, Harleen and Baldwin, Ian T. and Galis, Ivan}
}
