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Christopher Catanzaro*, Haval Kamake, and Sarabjit Bhatti

Twenty-one commercially introduced or trial cultivars of poinsettia (Euphorbia pulcherrima Willd. ex Klotzsch) supplied by Dummen USA or Ecke were grown at the TSU main campus farm during Autumn 2003. Ten plants of each cultivar were potted in 6-inch standard containers and grown from rooted cuttings to finished plants according to industry cultural practices in a glass greenhouse. Plant heights were recorded weekly. The date on which anthers began to shed pollen (flowering date) was recorded to calculate response time after initiation of short days. Also recorded on the flowering date were final plant height and two measurements of plant width and inflorescence width. Most cultivars finished within two weeks of the predicted response time of 7.5-9 weeks. However, flowers of `Infinity Red', `Merlot', `Mirage', and `Premium Marble' shed pollen especially late. Flower structures aborted on `Prestige', `Elegance Hot Pink' and `Premium Hot Pink'. Most cultivars were relatively compact at finish date. `Twister', `EuroGlory', and `Coco 2000 White' were particularly small, with average heights of 28-30 cm and average widths of 17 cm or less. `Spotlight Dark Red' was tallest (37cm) and widest (41cm), and also had the widest inflorescences (26 cm). Quality issues observed on some cultivars included low inflorescence number, excessive bract overlap, bract burn, bract reversion, high height to width ratio, and low plant vigor. Cultivars with overall high quality performance included `Premium Red', `Infinity Red', `Spotlight Dark Red', `Coco 2000 Red', and `Freedom', which all scored highly in the consumer preference survey conducted at the end of the study.

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Christopher Catanzaro*, Haval Kamake, and Sarabjit Bhatti

A poinsettia (Euphorbia pulcherrima Willd. ex Klotzsch) open house was held at the TSU main campus farm in Dec. 2003, during which a high quality finished plant of each of 21 cultivars was on display (supplied by Dummen USA and Ecke in August as rooted cuttings). The cultivars varied in inflorescence color and pattern, plant size and plant growth habit. Members of the campus community, the Tennessee Flower Growers Association, extension personnel, and the general public attended. Most attendees completed a written survey (n = 173), in which they rated how strongly they liked or disliked each cultivar. Cultivars were rated on a Likert-type scale (1 = strongly dislike, 7 = strongly like). Highly rated cultivars (mean >6) included `Premium Red', `Infinity Red', `Spotlight Dark Red', `Coco 2000 Red', `Merlot', `Prestige', `Freedom', and `Premium Hot Pink'. Less preferred (mean <4.4) were `Premium Marble', `Mirage', and `Limelight'. Although no cultivars were strongly disliked, the large, traditional red cultivars were preferred. Attendees also provided information on demographics and plant purchases. The typical attendee was a 40- to 59-year-old female with a college education and 2 to 3 people in the household with a total income of $25,000-50,000. Eighty percent bought poinsettias in 2002, with an average of 3.7 plants purchased. Eighty percent of plants purchased were red, and color was the most important selection feature. Results suggest that although most consumers prefer traditional red cultivars, a niche market exists for plants with novel inflorescence colors and unique bract and leaf coloration patterns and shapes.

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Suping Zhou, Marsha Palmer, Jing Zhou, Sarabjit Bhatti, Kevin J. Howe, Tara Fish, and Theodore W. Thannhauser

A comparative proteomics study using isobaric tags for relative and absolute quantitation (iTRAQ) was performed on a mesophytic tomato (Solanum lycopersicum) cultivar and a dehydration-resistant wild species (Solanum chilense) to identify proteins that play key roles in tolerance to water deficit stress. In tomato ‘Walter’ LA3465, 130 proteins were identified, of which 104 (80%) were repressed and 26 (20%) were induced. In S. chilense LA1958, a total of 170 proteins were identified with 106 (62%) repressed and 64 (38%) induced. According to their putative molecular functions, the differentially expressed proteins belong to the following subgroups: stress proteins, gene expression, nascent protein processing, protein folding, protein degradation, carbohydrate metabolism, amino acid and nucleotide metabolism, lipid metabolism, signal transduction, and cell cycle regulation. Based on changes in protein abundance induced by the dehydration treatment, cellular metabolic activities and protein biosynthesis were suppressed by the stress. In S. chilense, dehydration treatment led to elevated accumulation of proteins involved in post-transcriptional gene regulation and fidelity in protein translation including prefoldin, which promotes protein folding without the use of adenosine-5′-triphosphate (ATP), several hydrophilic proteins, and calmodulin in the calcium signal transduction pathway. Those protein changes were not found in the susceptible tomato, ‘Walter’. Within each functional protein group, proteins showing opposite changes (dehydration induced vs. repressed) in the two species were identified and roles of those proteins in conferring tolerance to water deficit stress are discussed. Information provided in this report will be useful for selection of proteins or genes in analyzing or improving dehydration tolerance in tomato cultivars.

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Suping Zhou, Roger J. Sauvé, Zong Liu, Sasikiran Reddy, Sarabjit Bhatti, Simon D. Hucko, Tara Fish, and Theodore W. Thannhauser

This article reports salt-induced changes in leaf and root proteomes after wild tomato (Solanum chilense) plants were treated with 200 mm NaCl. In leaf tissues, a total of 176 protein spots showed significant changes (P < 0.05), of which 104 spots were induced and 72 spots suppressed. Salt-induced proteins are associated with the following pathways: photosynthesis, carbohydrate metabolism, glyoxylate shunt, glycine cleavage system, branched-chain amino acid biosynthesis, protein folding, defense and cellular protection, signal transduction, ion transport, and antioxidant activities. Suppressed proteins belong to the following categories: oxidative phosphorylation pathway, photorespiration and protein translational machinery, oxidative stress, and ATPases. In root tissues, 106 protein spots changed significantly (P < 0.05) after the salt treatment, 63 spots were induced, and 43 suppressed by salt treatment. Salt-induced proteins are associated with the following functional pathways: regeneration of S-adenosyl methionine, protein folding, selective ion transport, antioxidants and defense mechanism, signal transduction and gene expression regulation, and branched-chain amino acid synthesis. Salt-suppressed proteins are receptor kinase proteins, peroxidases and germin-like proteins, malate dehydrogenase, and glycine dehydrogenase. In this study, different members of proteins were identified from leaf and root tissues after plants were subjected to salt treatment. These proteins represent tissue-specific changes in salt-induced proteomes. When protein expression was compared in the context of metabolic pathways, the branched-chain amino acid biosynthesis, glucose catabolism toward reducing cellular glucose level, and the antioxidant, detoxification, and selective ion uptake and transport were induced in both root and leaf tissues. These changes appear to be associated with salt tolerance in the whole plant.

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Suping Zhou, Roger J. Sauvé, Zong Liu, Sasikiran Reddy, Sarabjit Bhatti, Simon D. Hucko, Yang Yong, Tara Fish, and Theodore W. Thannhauser

Three tomato (Solanum lycopersicum) cultivars [Walter LA3465 (heat-tolerant), Edkawi LA 2711 (unknown heat tolerance, salt-tolerant), and LA1310 (cherry tomato)] were compared for changes in leaf proteomes after heat treatment. Seedlings with four fully expanded leaves were subjected to heat treatment of 39/25 °C at a 16:8 h light–dark cycle for 7 days. Leaves were collected at 1200 hr, 4 h after the light cycle started. For ‘Walter’ LA3465, heat-suppressed proteins were geranylgeranyl reductase, ferredoxin-NADP (+) reductase, Rubisco activase, transketolase, phosphoglycerate kinase precursor, fructose–bisphosphate aldolase, glyoxisomal malate dehydrogenase, catalase, S-adenosyl-L-homocysteine hydrolase, and methionine synthase. Two enzymes were induced, cytosolic NADP-malic enzyme and superoxide dismutase. For ‘Edkawi’ LA2711, nine enzymes were suppressed: ferredoxin-NADP (+) reductase, Rubisco activase, S-adenosylmethionine synthetase, methioine synthase, glyoxisomal malate dehydrogenase, enolase, flavonol synthase, M1 family peptidase, and dihydrolipoamide dehydrogenase. Heat-induced proteins were cyclophilin, fructose-1,6-bisphosphate aldolase, transketolase, phosphoglycolate phosphatase, ATPase, photosystem II oxygen-evolving complex 23, and NAD-dependent epimerase/dehydratase. For cherry tomato LA1310, heat-suppressed proteins were aminotransferase, S-adenosyl-L-homocysteine hydrolase, L-ascorbate peroxidase, lactoylglutathione lyase, and Rubisco activase. Heat-induced enzymes were glyoxisomal malate dehydrogenase, phosphoribulokinasee, and ATP synthase. This research resulted in the identification of proteins that were induced/repressed in all tomato cultivars evaluated (e.g., Rubisco activase, methionine synthase, adenosyl-L-homocysteine hydrolase, and others) and those differentially expressed (e.g., transketolase).