DOCSLIB.ORG

Proteomic Analysis of the Flavonoid Biosynthetic Machinery in Arabidopsis Thaliana

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Proteomic Analysis of the Flavonoid Biosynthetic Machinery in Arabidopsis Thaliana PROTEOMIC ANALYSIS OF THE FLAVONOID BIOSYNTHETIC MACHINERY IN ARABIDOPSIS THALIANA Nileshwari N. Vaghela Thesis submitted to the faculty of the Virginia Polytechnic Institute and State University in the partial fulfillment of the requirement for the degree of Master of Science in Biological Sciences Brenda S.J. Winkel, Ph.D., Committee Co-chair Iuliana M. Lazar, Ph.D., Committee Co-chair Richard F. Helm, Ph.D., Committee Member Richard A. Walker, Ph.D., Committee Member August 28, 2007 Blacksburg, Virginia Keywords: Protein-protein interactions, Enzyme complexes, Affinity chromatography, Flavonoid pathway, Mass spectrometry, Proteomics Copyright 2007, Nileshwari N. Vaghela PROTEOMIC ANALYSIS OF FLAVONOID BIOSYNTHETIC MACHINERY IN ARABIDOPSIS THALIANA Nileshwari N. Vaghela Abstract Work on a wide variety of metabolic pathways indicates that these systems are often, if not always, organized as multienzyme complexes. Enzyme complexes have the potential to increase catalytic efficiency and provide unique mechanisms for the regulation of cellular metabolism. The flavonoid biosynthetic pathway of Arabidopsis is an excellent model for studying the organization, localization, and regulation of enzyme complexes at the cellular level. Flavonoids are specialized metabolites that perform many important physiological roles in plants. Protein interactions among several key flavonoid enzymes have been described. Moreover, at least two of the flavonoid enzymes have a dual cytoplasmic/nuclear localization. These results indicate that flavonoid enzymes assemble into one or more distinct complexes at different intracellular locations. The current study integrates a new technology, mass spectrometry, with well-established affinity chromatography methods to further characterize the organization and composition of the Arabidopsis flavonoid enzyme complex. One of the key flavonoid enzymes, chalcone isomerase (CHI), was used in these experiments to detect interacting enzymes. Recombinant thioredoxin (TRX), or TRX-CHI, was produced in E. coli , then purified by metal affinity chromatography, and covalently coupled to an activated resin, Affi-Gel 10. Extracts prepared from 4-day-old wild type or CHI-deficient lines of Arabidopsis were then passed over the column and the bound proteins eluted with sodium dedocyl sulfate (SDS). This eluate was then subjected to a liquid chromatography (LC) - mass spectrometry (MS) protocol developed for the analysis of complex peptide mixtures. An Agilent LC system coupled with an LTQ-MS instrument (Thermo Electron, San Jose, CA) was used for this purpose. Data analysis was performed with the Bioworks software package. Different optimization strategies were performed to improve the affinity chromatography, sample preparation, and the LC separation method. A novel approach has been developed for the MS analysis of biological samples containing contaminants such as salts and detergents. Protein extracts prepared from wild type Landsburg and mutant tt5 (86) were analyzed by LC-MS/MS. A total of 491 proteins were identified for Landsburg and 633 for tt5 (86) extracts using a combination of data filters and p-value sorting. All detected proteins had p<0.001 and most were identified by at least 2 unique peptides. iii ACKNOWLEDGMENTS I wish to express my deepest gratitude to my mentors, Dr. Brenda S.J. Winkel and Dr. Iuliana M. Lazar, for giving me the opportunity to be part of the fascinating world of science and molecular biology and proteomics research. I thank them for encouraging me in many aspects of my research project, from challenging me in developing ideas, planning and executing experiments, to interpreting and presenting results. I would like to extend my thanks to my committee members, Dr. Richard F. Helm and Dr. Richard A. Walker for their time, contributions, and recommendations. I appreciate their willingness to serve on my research committee. My sincere thanks to my fellow lab mates in the Winkel laboratory, Melissa Ramirez, Jonathan Watkinson, Peter Bowerman, and Kevin Crosby, for their cheerful team spirit and support. In addition, I would also like to thank Hetal Sarvaiya and Dr. Jung Hae Yoon for their help with mass spectrometric research. My deepest gratitude belongs to my family for being endlessly supportive and caring. My sister-in-law, Nirali for helping me and motivating during my graduate career. I would like to thank my husband, Nishant for always believing in me and helping me reach my goals. Without him I would not be where I am today. This work is dedicated to him. iv A special thanks to my friend, Dr. Margret S. Rodrigues, for her help in reviewing my thesis and motivating me to reach my goal. v CONTENTS ACKNOWLEDGMENTS ................................................................................................. iv TABLE OF CONTENTS................................................................................................... vi LIST OF FIGURES ......................................................................................................... viii LIST OF TABLES.............................................................................................................. x Chapter 1 : Introduction ......................................................................................................1 Multienzyme Complexes .....................................................................................................2 The Flavonoid Biosynthetic Pathway of Arabidopsis thaliana ...........................................2 Mass Spectrometry...............................................................................................................6 Protein Profiling by Mass Spectrometry............................................................................10 Protein-Protein Interactions and Proteomics .....................................................................10 Proposed Study ..................................................................................................................12 Acknowledgments..............................................................................................................13 Chapter 2 : Proteomic Analysis of the Flavonoid Biosynthetic Machinery of Arabidopsis thaliana .............................................................................................................14 Summary............................................................................................................................15 Introduction........................................................................................................................16 Materials and Methods.......................................................................................................18 Results................................................................................................................................20 Discussion..........................................................................................................................23 Acknowledgment ...............................................................................................................23 vi Chapter 3 : Mass Spectrometric Analysis of Recombinant Proteins, Affinity Eluted Samples, and Soluble Plant Extracts From Wild Type Landsburg Ecotype and Mutant tt5 (86) Arabidopsis thaliana .........................................................................................................24 Summary............................................................................................................................25 Introduction........................................................................................................................26 Materials and Methods.......................................................................................................27 Results................................................................................................................................31 Discussion..........................................................................................................................51 Acknowledgments..............................................................................................................52 Chapter 4 : Conclusions ....................................................................................................53 Conclusions........................................................................................................................54 References..........................................................................................................................56 Appendix A: Results from proteomic analysis of Landsburg seedlings............................68 VITA..................................................................................................................................79 vii List of Figures Chapter 1 Figure 1.1 Phenotypic changes induced by transparent testa (tt ) mutation. .......................4 Figure 1.2 Schematic of the flavonoid pathway of Arabidopsis.........................................5 Figure 1.3 Schematic representation of the main processes occurring within a mass spectrometer. ..........................................................................................8 Figure 1.4 Outline of the protein identification process. ....................................................9 Chapter 2 Figure 2.1 Schematic diagram of experimental steps performed for affinity chromatography and mass spectrometry..........................................................17
Load more

Recommended publications
  • Itraq-Based Quantitative Proteomics Analysis Reveals the Mechanism Underlying the Weakening of Carbon Metabolism in Chlorotic Tea Leaves
    Article iTRAQ-Based Quantitative Proteomics Analysis Reveals the Mechanism Underlying the Weakening of Carbon Metabolism in Chlorotic Tea Leaves Fang Dong 1,2, Yuanzhi Shi 1,2, Meiya Liu 1,2, Kai Fan 1,2, Qunfeng Zhang 1,2,* and Jianyun Ruan 1,2 1 Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou 310008, China; [email protected] (F.D.); [email protected] (Y.S.); [email protected] (M.L.); [email protected] (K.F.); [email protected] (J.R.) 2 Key Laboratory for Plant Biology and Resource Application of Tea, the Ministry of Agriculture, Hangzhou 310008, China * Correspondence: [email protected]; Tel.: +86-571-8527-0665 Received: 7 November 2018; Accepted: 5 December 2018; Published: 7 December 2018 Abstract: To uncover mechanism of highly weakened carbon metabolism in chlorotic tea (Camellia sinensis) plants, iTRAQ (isobaric tags for relative and absolute quantification)-based proteomic analyses were employed to study the differences in protein expression profiles in chlorophyll-deficient and normal green leaves in the tea plant cultivar “Huangjinya”. A total of 2110 proteins were identified in “Huangjinya”, and 173 proteins showed differential accumulations between the chlorotic and normal green leaves. Of these, 19 proteins were correlated with RNA expression levels, based on integrated analyses of the transcriptome and proteome. Moreover, the results of our analysis of differentially expressed proteins suggested that primary carbon metabolism (i.e., carbohydrate synthesis and transport) was inhibited in chlorotic tea leaves. The differentially expressed genes and proteins combined with photosynthetic phenotypic data indicated that 4-coumarate-CoA ligase (4CL) showed a major effect on repressing flavonoid metabolism, and abnormal developmental chloroplast inhibited the accumulation of chlorophyll and flavonoids because few carbon skeletons were provided as a result of a weakened primary carbon metabolism.
    [Show full text]
  • Structure of Pigment Metabolic Pathways and Their Contributions to White Tepal Color Formation of Chinese Narcissus Tazetta Var
    International Journal of Molecular Sciences Article Structure of Pigment Metabolic Pathways and Their Contributions to White Tepal Color Formation of Chinese Narcissus tazetta var. chinensis cv Jinzhanyintai Yujun Ren † ID , Jingwen Yang †, Bingguo Lu, Yaping Jiang, Haiyang Chen, Yuwei Hong, Binghua Wu and Ying Miao * Center for Molecular Cell and Systems Biology, Fujian Provincial Key Laboratory of Haixia Applied Plant Systems Biology, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China; [email protected] (Y.R.); [email protected] (J.Y.); [email protected] (B.L.); [email protected] (Y.J.); [email protected] (H.C.); [email protected] (Y.H.); [email protected] (B.W.) * Correspondence: [email protected]; Tel.:/Fax: +86-591-8639-2987 † These authors contributed equally to this work. Received: 7 August 2017; Accepted: 4 September 2017; Published: 8 September 2017 Abstract: Chinese narcissus (Narcissus tazetta var. chinensis) is one of the ten traditional flowers in China and a famous bulb flower in the world flower market. However, only white color tepals are formed in mature flowers of the cultivated varieties, which constrains their applicable occasions. Unfortunately, for lack of genome information of narcissus species, the explanation of tepal color formation of Chinese narcissus is still not clear. Concerning no genome information, the application of transcriptome profile to dissect biological phenomena in plants was reported to be effective. As known, pigments are metabolites of related metabolic pathways, which dominantly decide flower color. In this study, transcriptome profile and pigment metabolite analysis methods were used in the most widely cultivated Chinese narcissus “Jinzhanyintai” to discover the structure of pigment metabolic pathways and their contributions to white tepal color formation during flower development and pigmentation processes.
    [Show full text]
  • Reductase from Populus Trichocarpa
    Isolation and Characterization of cDNAs Encoding Leucoanthocyanidin Reductase and Anthocyanidin Reductase from Populus trichocarpa Lijun Wang1,2., Yuanzhong Jiang1., Li Yuan1., Wanxiang Lu2,3, Li Yang1, Abdul Karim1, Keming Luo1,2,3* 1 Key Laboratory of Eco-environments of Three Gorges Reservoir Region, Ministry of Education, Institute of Resources Botany, School of Life Sciences, Southwest University, Chongqing, China, 2 College of Horticulture and Landscape Architecture, Southwest University, Chongqing, China, 3 Key Laboratory of Adaptation and Evolution of Plateau Biota, Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining, China Abstract Proanthocyanidins (PAs) contribute to poplar defense mechanisms against biotic and abiotic stresses. Transcripts of PA biosynthetic genes accumulated rapidly in response to infection by the fungus Marssonina brunnea f.sp. multigermtubi, treatments of salicylic acid (SA) and wounding, resulting in PA accumulation in poplar leaves. Anthocyanidin reductase (ANR) and leucoanthocyanidin reductase (LAR) are two key enzymes of the PA biosynthesis that produce the main subunits: (+)-catechin and (2)-epicatechin required for formation of PA polymers. In Populus, ANR and LAR are encoded by at least two and three highly related genes, respectively. In this study, we isolated and functionally characterized genes PtrANR1 and PtrLAR1 from P. trichocarpa. Phylogenetic analysis shows that Populus ANR1 and LAR1 occurr in two distinct phylogenetic lineages, but both genes have little difference in their tissue distribution, preferentially expressed in roots. Overexpression of PtrANR1 in poplar resulted in a significant increase in PA levels but no impact on catechin levels. Antisense down-regulation of PtrANR1 showed reduced PA accumulation in transgenic lines, but increased levels of anthocyanin content.
    [Show full text]
  • Proanthocyanidin Synthesis in Theobroma Cacao: Genes Encoding
    Liu et al. BMC Plant Biology 2013, 13:202 http://www.biomedcentral.com/1471-2229/13/202 RESEARCH ARTICLE Open Access Proanthocyanidin synthesis in Theobroma cacao: genes encoding anthocyanidin synthase, anthocyanidin reductase, and leucoanthocyanidin reductase Yi Liu1,4, Zi Shi1, Siela Maximova2, Mark J Payne3 and Mark J Guiltinan2* Abstract Background: The proanthocyanidins (PAs), a subgroup of flavonoids, accumulate to levels of approximately 10% total dry weight of cacao seeds. PAs have been associated with human health benefits and also play important roles in pest and disease defense throughout the plant. Results: To dissect the genetic basis of PA biosynthetic pathway in cacao (Theobroma cacao), we have isolated three genes encoding key PA synthesis enzymes, anthocyanidin synthase (ANS), anthocyanidin reductase (ANR) and leucoanthocyanidin reductase (LAR). We measured the expression levels of TcANR, TcANS and TcLAR and PA content in cacao leaves, flowers, pod exocarp and seeds. In all tissues examined, all three genes were abundantly expressed and well correlated with PA accumulation levels, suggesting their active roles in PA synthesis. Overexpression of TcANR in an Arabidopsis ban mutant complemented the PA deficient phenotype in seeds and resulted in reduced anthocyanidin levels in hypocotyls. Overexpression of TcANS in tobacco resulted in increased content of both anthocyanidins and PAs in flower petals. Overexpression of TcANS in an Arabidopsis ldox mutant complemented its PA deficient phenotype in seeds. Recombinant TcLAR protein converted leucoanthocyanidin to catechin in vitro. Transgenic tobacco overexpressing TcLAR had decreased amounts of anthocyanidins and increased PAs. Overexpressing TcLAR in Arabidopsis ldox mutant also resulted in elevated synthesis of not only catechin but also epicatechin.
    [Show full text]
  • The Plant Short-Chain Dehydrogenase (SDR) Superfamily: Genome-Wide Inventory and Diversification Patterns
    Moummou et al. BMC Plant Biology 2012, 12:219 http://www.biomedcentral.com/1471-2229/12/219 RESEARCH ARTICLE Open Access The Plant Short-Chain Dehydrogenase (SDR) superfamily: genome-wide inventory and diversification patterns Hanane Moummou1,2, Yvonne Kallberg3, Libert Brice Tonfack1,4, Bengt Persson5,6 and Benoît van der Rest1,7* Abstract Background: Short-chain dehydrogenases/reductases (SDRs) form one of the largest and oldest NAD(P)(H) dependent oxidoreductase families. Despite a conserved ‘Rossmann-fold’ structure, members of the SDR superfamily exhibit low sequence similarities, which constituted a bottleneck in terms of identification. Recent classification methods, relying on hidden-Markov models (HMMs), improved identification and enabled the construction of a nomenclature. However, functional annotations of plant SDRs remain scarce. Results: Wide-scale analyses were performed on ten plant genomes. The combination of hidden Markov model (HMM) based analyses and similarity searches led to the construction of an exhaustive inventory of plant SDR. With 68 to 315 members found in each analysed genome, the inventory confirmed the over-representation of SDRs in plants compared to animals, fungi and prokaryotes. The plant SDRs were first classified into three major types —‘classical’, ‘extended’ and ‘divergent’—but a minority (10% of the predicted SDRs) could not be classified into these general types (‘unknown’ or ‘atypical’ types). In a second step, we could categorize the vast majority of land plant SDRs into a set of 49 families. Out of these 49 families, 35 appeared early during evolution since they are commonly found through all the Green Lineage. Yet, some SDR families — tropinone reductase-like proteins (SDR65C), ‘ABA2-like’-NAD dehydrogenase (SDR110C), ‘salutaridine/menthone-reductase-like’ proteins (SDR114C), ‘dihydroflavonol 4-reductase’-like proteins (SDR108E) and ‘isoflavone-reductase-like’ (SDR460A) proteins — have undergone significant functional diversification within vascular plants since they diverged from Bryophytes.
    [Show full text]
  • Molecular Profiling of Pierce's Disease Outlines the Response Circuitry Of
    fpls-09-00771 June 6, 2018 Time: 16:19 # 1 ORIGINAL RESEARCH published: 08 June 2018 doi: 10.3389/fpls.2018.00771 Molecular Profiling of Pierce’s Disease Outlines the Response Circuitry of Vitis vinifera to Xylella fastidiosa Infection Paulo A. Zaini1†, Rafael Nascimento2†, Hossein Gouran1, Dario Cantu3, Sandeep Chakraborty1, My Phu1, Luiz R. Goulart2 and Abhaya M. Dandekar1* 1 Department of Plant Sciences, University of California, Davis, Davis, CA, United States, 2 Institute of Genetics and Biochemistry, Federal University of Uberlândia, Uberlândia, Brazil, 3 Department of Viticulture and Enology, University of California, Davis, Davis, CA, United States Pierce’s disease is a major threat to grapevines caused by the bacterium Xylella fastidiosa. Although devoid of a type 3 secretion system commonly employed by bacterial pathogens to deliver effectors inside host cells, this pathogen is able to influence host parenchymal cells from the xylem lumen by secreting a battery of hydrolytic enzymes. Defining the cellular and biochemical changes induced during Edited by: disease can foster the development of novel therapeutic strategies aimed at reducing Glória Catarina Pinto, the pathogen fitness and increasing plant health. To this end, we investigated University of Aveiro, Portugal the transcriptional, proteomic, and metabolomic responses of diseased Vitis vinifera Reviewed by: compared to healthy plants. We found that several antioxidant strategies were induced, Jorge Martin-Garcia, University of Valladolid, Spain including the accumulation of gamma-aminobutyric acid (GABA) and polyamine Mónica Meijón, metabolism, as well as iron and copper chelation, but these were insufficient to protect Universidad de Oviedo, Spain the plant from chronic oxidative stress and disease symptom development.
    [Show full text]
  • A New Buckwheat Dihydroflavonol 4-Reductase (DFR), with a Unique
    Katsu et al. BMC Plant Biology (2017) 17:239 DOI 10.1186/s12870-017-1200-6 RESEARCH ARTICLE Open Access A new buckwheat dihydroflavonol 4-reductase (DFR), with a unique substrate binding structure, has altered substrate specificity Kenjiro Katsu1, Rintaro Suzuki2, Wataru Tsuchiya2, Noritoshi Inagaki2, Toshimasa Yamazaki2, Tomomi Hisano1, Yasuo Yasui3, Toshiyuki Komori4, Motoyuki Koshio4, Seiji Kubota4, Amanda R. Walker5, Kiyoshi Furukawa4 and Katsuhiro Matsui1,6* Abstract Background: Dihydroflavonol 4-reductase (DFR) is the key enzyme committed to anthocyanin and proanthocyanidin biosynthesis in the flavonoid biosynthetic pathway. DFR proteins can catalyse mainly the three substrates (dihydrokaempferol, dihydroquercetin, and dihydromyricetin), and show different substrate preferences. Although relationships between the substrate preference and amino acids in the region responsible for substrate specificity have been investigated in several plant species, the molecular basis of the substrate preference of DFR is not yet fully understood. Results: By using degenerate primers in a PCR, we isolated two cDNA clones that encoded DFR in buckwheat (Fagopyrum esculentum). Based on sequence similarity, one cDNA clone (FeDFR1a)wasidenticaltotheFeDFR in DNA databases (DDBJ/Gen Bank/EMBL). The other cDNA clone, FeDFR2, had a similar sequence to FeDFR1a,buta different exon-intron structure. Linkage analysis in an F2 segregating population showed that the two loci were linked. Unlike common DFR proteins in other plant species, FeDFR2 contained a valine instead of the typical asparagine at the third position and an extra glycine between sites 6 and 7 in the region that determines substrate specificity, and showed less activity against dihydrokaempferol than did FeDFR1a with an asparagine at the third position.
    [Show full text]
  • Comparative Transcriptome Analysis of Grapevine in Response to Copper
    www.nature.com/scientificreports OPEN Comparative transcriptome analysis of grapevine in response to copper stress Received: 27 March 2015 Accepted: 05 November 2015 Xiangpeng Leng, Haifeng Jia, Xin Sun, Lingfei Shangguan, Qian Mu, Baoju Wang & Published: 17 December 2015 Jinggui Fang Grapevine is one of the most economically important and widely cultivated fruit crop worldwide. With the industrialization and the popular application of cupric fungicides in grape industry, copper stress and copper pollution are also the factors affecting grape production and berry and wine quality. Here, 3,843 transcripts were significantly differently expressed genes in response to Cu stress by RNA-seq, which included 1,892 up-regulated and 1,951 down-regulated transcripts. During this study we found many known and novel Cu-induced and -repressed genes. Biological analysis of grape samples were indicated that exogenous Cu can influence chlorophylls metabolism and photosynthetic activities of grapevine. Most ROS detoxification systems, including antioxidant enzyme, stress-related proteins and secondary metabolites were strongly induced. Concomitantly, abscisic acid functioned as a negative regulator in Cu stress, in opposite action to ethylene, auxin, jasmonic acid, and brassinolide. This study also identified a set of Cu stress specifically activated genes coding copper transporter, P1B-type ATPase, multidrug transporters. Overall, this work was carried out to gain insights into the copper-regulated and stress-responsive mechanisms in grapevine at transcriptome level. This research can also provide some genetic information that can help us in better vinery management and breeding Cu-resistant grape cultivars. Copper (Cu) is an important micronutrient essential for plant growth and plays a key role in many phys- iological processes, including photosynthetic and respiratory electron-transport chains, C and N metab- olism ratio, hormone perception, cell wall metabolism and oxidative stress protection1–3.
    [Show full text]
  • Ziziphus Jujuba Mill.) During Different Cite This: RSC Adv.,2021,11, 22106 Growth Stages†
    RSC Advances View Article Online PAPER View Journal | View Issue Label-free quantitative proteomics analysis of jujube (Ziziphus jujuba Mill.) during different Cite this: RSC Adv.,2021,11, 22106 growth stages† Xiaoli Huang and Zhaohua Hou * Chinese jujube (Zizyphus jujuba Mill.), a member of the Rhamnaceae family with favorable nutritional and flavor quality, exhibited characteristic climacteric changes during its fruit growth stage. Therefore, fruit samples were harvested at four developmental stages on days 55 (young fruits), 76 (white-mature fruits), 96 (half-red fruits), and 116 (full-red fruits) after flowering (DAF). This study then investigated those four growth stage changes of the jujube proteome using label-free quantification proteomics. The results identified 4762 proteins in the samples, of which 3757 proteins were quantified. Compared with former stages, the stages examined were designated as “76 vs. 55 DAF” group, “96 vs. 76 DAF” group, and “116 vs. 96 DAF” group. Gene Ontology (GO) and KEGG annotation and enrichment analysis of the Creative Commons Attribution 3.0 Unported Licence. differentially expressed proteins (DEPs) showed that 76 vs. 55 DAF group pathways represented amino sugar, nucleotide sugar, ascorbate, and aldarate metabolic pathways. These pathways were associated with cell division and resistance. In the study, the jujube fruit puffing slowed down and attained a stable growth stage in the 76 vs. 55 DAF group. However, fatty acid biosynthesis and phenylalanine metabolism was mainly enriched in the 96 vs. 76 DAF group. Fatty acids are precursors of aromatic substances and fat-soluble pigments in fruit. The upregulation of differential proteins at this stage indicates that aromatic compounds were synthesized in large quantities at this stage and that fruit would enter the ripening stage.
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • Generate Metabolic Map Poster
    Authors: Aureliano Bombarely, Boyce Thompson Institute LycoCyc: Solanum lycopersicum Cellular Overview Lukas Mueller, Boyce Thompson Institute a xenobiotic a xenobiotic a xenobiotic a xenobiotic + a xenobiotic a xenobiotic H phosphonate 2+ an a xenobiotic a xenobiotic ABC a xenobiotic a xenobiotic a xenobiotic ABC a xenobiotic Cd a xenobiotic a xenobiotic a xenobiotic ABC a xenobiotic ABC a xenobiotic a xenobiotic a xenobiotic oligopeptide a xenobiotic a xenobiotic Cd 2+ a xenobiotic sucrose a xenobiotic transporter transporter transporter transporter sucrose H + a xenobiotic a xenobiotic C family C family C family C family a xenobiotic a xenobiotic ABC a xenobiotic a xenobiotic a xenobiotic a xenobiotic a xenobiotic Macrolide ABC a xenobiotic sucrose H(+)-ATPase H + member 4/ member 8/ a xenobiotic member 10/ member 10/ Cu 2+ H + transporter ABC export ATP- ABC transporter 4//H(\+)- ABC /Multidrug ABC ABC ABC /Multidrug ABC Cadmium- ABC ABC ABC /Multidrug ABC /Multidrug ABC ABC ABC Sucrose C family transporter ABC binding/ transporter B family Sucrose transporting transporter ABC resistance transporter transporter transporter resistance transporter transporting Cadmium/zinc- ABC transporter transporter transporter resistance transporter resistance transporter transporter transporter transport ABC transporter member 2/ I family transporter permease B family member transport Sucrose ATP synthase atpase plant/ MATE efflux ABC C family transporter protein ABC C family C family C family protein ABC C family ATPase// transporting transporter
    [Show full text]
  • Insights Into Grapevine Defense Response Against Drought As
    bioRxiv preprint doi: https://doi.org/10.1101/065136; this version posted December 19, 2016. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Insights into grapevine defense response against drought as revealed by biochemical, 2 physiological and RNA-Seq analysis 3 Muhammad Salman Haider, Cheng Zhang, Mahantesh M. Kurjogi Tariq Pervaiz, Ting Zheng, 4 Chao bo Zhang, Chen Lide, Lingfie Shangguan, Jinggui Fang* 5 College of Horticulture, Nanjing Agricultural University, Tongwei Road 6, Nanjing 210095, PR. 6 China 7 *Corresponding author 8 Jinggui Fang 9 Email: [email protected] 10 Abstract 11 Grapevine is economically important and widely cultivated fruit crop, which is seriously 12 hampered by drought worldwide. It is necessary to understand the impact of glitches incurred by 13 the drought on grapevine genetic resources. Therefore, in the present study RNA-sequencing 14 analysis was performed using cDNA libraries constructed from both drought-stress and control 15 plants. Results yielded, a total of 12,451 differentially expressed genes (DEGs) out of which 16 8,022 genes were up-regulated and 4,430 were down-regulated. Further physiological and 17 biochemical analyses were carried out to validate the various biological processes involved in the 18 development of grapevine in response to drought stress. Results also showed that decrease in rate 19 of stomatal conductance in-turn decrease the photosynthetic activity and CO2 assimilation rate in 20 the grapevine leaves and most ROS detoxification systems, including stress enzymes, stress- 21 related proteins and secondary metabolites were strongly induced.
    [Show full text]