DOCSLIB.ORG

Type III Polyketide Synthases from Gerbera Hybrida

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Type III Polyketide Synthases from Gerbera Hybrida DISSERTATIONES SCHOLA DOCTORALIS SCIENTIAE CIRCUMIECTALIS, ALIMENTARIAE, BIOLOGICAE. UNIVERSITATIS HELSINKIENSIS 2/2017 JUHA KONTTURI Type III Polyketide Synthases from Gerbera hybrida DEPARTMENT OF AGRICULTURAL SCIENCES FACULTY OF AGRICULTURE AND FORESTRY DOCTORAL PROGRAMME IN PLANT SCIENCES UNIVERSITY OF HELSINKI Type III Polyketide Synthases from Gerbera Hybrida Juha Kontturi Biotechnology Doctoral school in Plant Sciences Department of Agricultural Sciences Faculty of Agriculture and Forestry University of Helsinki ACADEMIC DISSERTATION To be presented, with the permission of the Faculty of Agriculture and Forestry of the University of Helsinki, for public examination in the lecture room B6 (Metsätieteiden talo, Latokartanonkaari 7) on 10th of February 2017 at 12 o’clock. Supervisor: Professor Teemu Teeri Department of Agricultural Sciences University of Helsinki Follow-up group: Docent Jussi Joensuu VTT Technical Research Centre of Finland Doctor Milla Pietiäinen University of Helsinki Reviewers: Docent/Principal Scientist Anneli Ritala VTT Technical Research Centre Finland Professor Rob Veerporte University of Leiden Opponent: Doctor Günter Brader Austrian Institute of Technology Custos: Professor Teemu Teeri Department of Agricultural Sciences University of Helsinki, Finland ISSN 2342-5423 ISBN 978-951-51-2949-9 (paperback) ISBN 978-951-51-2950-5 (PDF) ethesis.helsinki.fi Kiriprintti Oy 2017 2 CONTENTS ABBREVIATIONS ........................................................................................................................................... 5 LIST OF ORIGINAL PUBLICATIONS ................................................................................................................. 6 ABSTRACT .................................................................................................................................................... 7 1. INTRODUCTION........................................................................................................................................ 8 1.1 Type III Polyketide synthases (PKS) ..................................................................................................... 8 1.1.1 Chalcone synthase (CHS) ............................................................................................................10 1.1.2 Stilbene synthase (STS) ...............................................................................................................12 1.1.3 2-pyrone synthase (2PS) .............................................................................................................12 1.1.4 Pentaketide chromonesynthase (PCS) and Octaketidesynthase (OKS) .........................................12 1.1.5 Anther specific chalcone synthases (ASCLs) ................................................................................13 1.2 Type III PKS structure and function ....................................................................................................14 1.2.1 Engineering plant polyketides .....................................................................................................15 1.2.2 Combinatorial biosynthesis.........................................................................................................16 1.3 Type III PKSs in the biosynthesis of plant secondary metabolites .......................................................16 1.3.1 The biosynthesis of 4-hydroxy-5-methylcoumarin (HMC)............................................................16 1.3.2 The biosynthesis of sporopollenin ..............................................................................................18 1.4 Glycosylation of plant metabolites ....................................................................................................20 1.4.1 The function of GTs ....................................................................................................................20 1.4.2 The physiological role of GTs ......................................................................................................21 1.4.3 Structure of GTs .........................................................................................................................21 1.4.4 Protein engineering of GTs and biotechnological applications.....................................................22 2. AIMS OF THE STUDY ................................................................................................................................23 3. MATERIALS AND METHODS ....................................................................................................................23 4. RESULTS AND DISCUSSION ......................................................................................................................24 4.1 Characterization of new 2PS enzymes, G2PS2 and G2PS3 from Gerbera hybrida ...............................24 4.1.1 In vitro enzymatic activity of G2PS2 and G2PS3 ..........................................................................24 4.1.2 G2PS2 and G2PS3 expression in planta .......................................................................................25 4.1.3 Active site of G2PS2 and G2PS3 ..................................................................................................25 4.1.4 Enzyme activity of mutated G2PS1 and G2PS2 ............................................................................26 4.1.5 Expression patterns of G2PS2 and G2PS3....................................................................................26 3 4.2 Functional characterization of GASCL1 and GASCL2, two ASCL enzymes from Gerbera hybrida .........27 4.2.1 In vitro enzyme activity of GASCL1 and GASCL2 ..........................................................................27 4.2.2 Expression of GASCL1 and GASCL2 ..............................................................................................29 4.3 Characterization of gerbera GTs ........................................................................................................30 4.3.1 In vitro activity of gerbera GTs ....................................................................................................30 4.3.2 Virus induced gene silencing of glucosyltransferases ..................................................................30 5. CONCLUSION AND FUTURE PROSPECTS ..................................................................................................32 6. ACKNOWLEDGEMENTS ...........................................................................................................................33 7. REFERENCES ...........................................................................................................................................34 4 ABBREVIATIONS 2PS 2-pyrone synthase ASCL Anther specific chalcone synthase ALS Aloesone synthase ANS Anthocyanidin synthase Asn Asparagine AT Acyl transferase BAS Benzalacetone synthase BIS Biphenyl synthase cDNA Complementary DNA CHI Chalcone isomerase CHS Chalcone synthase CoA Coenzyme A CUR Curcuminoid synthase Cys Cysteine DFR Dihydroflavonol reductase ESI-MS Electron spray ionization mass spectrometry FAS Fatty acid synthase F3H Flavanone 3ɴ-hydroxylase F3´H Flavanoid 3’-hydroxylase FLS Flavonol synthase FNS Flavone synthase GT Glycosyltransferase Gly Glysine TAL Triacetolactone His Histidine Ile Isoleucine HMC 4-hydroxy-5-methylcoumarin HPLC High performance liquid chromatography HR Hypersensitive response KAS Ketoacyl synthase LAR Leucoanthocyanidin reductase Leu Leucine OAC Olivetolic acid cyclase OARS Oxoalkylresorcinol synthase OKS Octaketide synthase PCR Polymerase chain reaction PCS Pentaketide chromone synthase Phe Phenylalanine PKR Polyketide reductase PKS Polyketide synthase SA Salicylic acid Ser Serine STCS Stilbenecarboxylate synthase STS Stillbene synthase TAL Triacetolactone Thr Threonine TLC Thin-layer chromatography TKPR Tetraketide-2-pyrone reductase TMV Tobacco Mosaic Virus Tyr Tyrosine UDP Uridine-diphosphate UPLC Ultra performance liquid chromatography VIGS Virus Induced Gene Silencing 5 LIST OF ORIGINAL PUBLICATIONS The thesis is based on the following publications: I *Pietiäinen M., *Kontturi J., Paasela., Deng X., Ainasoja M., Nyberg P., Hotti H., Teeri T. 2016. Two polyketide synthases are necessary for 4-hydroxy-5-methylcoumarin biosynthesis in Gerbera hybrida. Plant Journal, 87: 548-558. II Kontturi J., Osama R., Deng X., Bashandy H., Albert V.A., Teeri T.H. 2017. Functional characterization and expression of GASCL1 and GASCL2, two anther-specific chalcone synthase like enzymes from Gerbera hybrida. Phytochemistry, 134: 38-45. III Kontturi J., Lampio A., Deng X., Teeri T.H. Glucosyltransferases from Gerbera hybrida. Manuscript. *Shared first authorship Contribution to the articles I I did the cloning of PKS genes, protein production in E.coli, protein purification and in vitro enzymatic assays. I did all the HPLC runs from in vitro assays and tobacco infiltration results, and with the help of MS-laboratory, analyzed the MS-results from all experiments. I did the protein models, mutagenesis, and all the work relating to the mutated proteins and in vitro results. Finally, I analyzed the transgenic gerbera plants for HMC. I participated in planning the experiments, and wrote the article with Milla Pietiäinen under the supervision of Teemu Teeri. II I cloned the PKS-genes, made protein production in E.coli, protein purification and in vitro enzymatic assays. I screened the results with HPLC and with the help of MS-laboratory,
Load more

Recommended publications
  • Health Effects Support Document for Perfluorooctanoic Acid (PFOA)
    United States Office of Water EPA 822-R-16-003 Environmental Protection Mail Code 4304T May 2016 Agency Health Effects Support Document for Perfluorooctanoic Acid (PFOA) Perfluorooctanoic Acid – May 2016 i Health Effects Support Document for Perfluorooctanoic Acid (PFOA) U.S. Environmental Protection Agency Office of Water (4304T) Health and Ecological Criteria Division Washington, DC 20460 EPA Document Number: 822-R-16-003 May 2016 Perfluorooctanoic Acid – May 2016 ii BACKGROUND The Safe Drinking Water Act (SDWA), as amended in 1996, requires the Administrator of the U.S. Environmental Protection Agency (EPA) to periodically publish a list of unregulated chemical contaminants known or anticipated to occur in public water systems and that may require regulation under SDWA. The SDWA also requires the Agency to make regulatory determinations on at least five contaminants on the Contaminant Candidate List (CCL) every 5 years. For each contaminant on the CCL, before EPA makes a regulatory determination, the Agency needs to obtain sufficient data to conduct analyses on the extent to which the contaminant occurs and the risk it poses to populations via drinking water. Ultimately, this information will assist the Agency in determining the most appropriate course of action in relation to the contaminant (e.g., developing a regulation to control it in drinking water, developing guidance, or deciding not to regulate it). The PFOA health assessment was initiated by the Office of Water, Office of Science and Technology in 2009. The draft Health Effects Support Document for Perfluoroctanoic Acid (PFOA) was completed in 2013 and released for public comment in February 2014.
    [Show full text]
  • Supplementary File 2A Revised
    Supplementary file 2A. Differentially expressed genes in aldosteronomas compared to all other samples, ranked according to statistical significance. Missing values were not allowed in aldosteronomas, but to a maximum of five in the other samples. Acc UGCluster Name Symbol log Fold Change P - Value Adj. P-Value B R99527 Hs.8162 Hypothetical protein MGC39372 MGC39372 2,17 6,3E-09 5,1E-05 10,2 AA398335 Hs.10414 Kelch domain containing 8A KLHDC8A 2,26 1,2E-08 5,1E-05 9,56 AA441933 Hs.519075 Leiomodin 1 (smooth muscle) LMOD1 2,33 1,3E-08 5,1E-05 9,54 AA630120 Hs.78781 Vascular endothelial growth factor B VEGFB 1,24 1,1E-07 2,9E-04 7,59 R07846 Data not found 3,71 1,2E-07 2,9E-04 7,49 W92795 Hs.434386 Hypothetical protein LOC201229 LOC201229 1,55 2,0E-07 4,0E-04 7,03 AA454564 Hs.323396 Family with sequence similarity 54, member B FAM54B 1,25 3,0E-07 5,2E-04 6,65 AA775249 Hs.513633 G protein-coupled receptor 56 GPR56 -1,63 4,3E-07 6,4E-04 6,33 AA012822 Hs.713814 Oxysterol bining protein OSBP 1,35 5,3E-07 7,1E-04 6,14 R45592 Hs.655271 Regulating synaptic membrane exocytosis 2 RIMS2 2,51 5,9E-07 7,1E-04 6,04 AA282936 Hs.240 M-phase phosphoprotein 1 MPHOSPH -1,40 8,1E-07 8,9E-04 5,74 N34945 Hs.234898 Acetyl-Coenzyme A carboxylase beta ACACB 0,87 9,7E-07 9,8E-04 5,58 R07322 Hs.464137 Acyl-Coenzyme A oxidase 1, palmitoyl ACOX1 0,82 1,3E-06 1,2E-03 5,35 R77144 Hs.488835 Transmembrane protein 120A TMEM120A 1,55 1,7E-06 1,4E-03 5,07 H68542 Hs.420009 Transcribed locus 1,07 1,7E-06 1,4E-03 5,06 AA410184 Hs.696454 PBX/knotted 1 homeobox 2 PKNOX2 1,78 2,0E-06
    [Show full text]
  • Molecular Architectures of Benzoic Acid-Specific Type III Polyketide Synthases
    research papers Molecular architectures of benzoic acid-specific type III polyketide synthases ISSN 2059-7983 Charles Stewart Jr,a,b* Kate Woods,a Greg Macias,a Andrew C. Allan,c,d Roger P. Hellensc,e and Joseph P. Noela aHoward Hughes Medical Institute, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA, bMacromolecular Received 11 July 2017 X-ray Crystallography Facility, Office of Biotechnology, Iowa State University, 0202 Molecular Biology Building, 2437 c Accepted 17 November 2017 Pammel Drive, Ames, IA 50011, USA, The New Zealand Institute for Plant and Food Research Limited (PFR), Auckland, New Zealand, dSchool of Biological Sciences, University of Auckland, Auckland, New Zealand, and eQueensland University of Technology, Brisbane, Queensland 4001, Australia. *Correspondence e-mail: [email protected] Edited by A. Berghuis, McGill University, Canada Biphenyl synthase and benzophenone synthase constitute an evolutionarily distinct clade of type III polyketide synthases (PKSs) that use benzoic acid- Keywords: chalcone synthase; biphenyl derived substrates to produce defense metabolites in plants. The use of benzoyl- synthase; benzophenone synthase; polyketide CoA as an endogenous substrate is unusual for type III PKSs. Moreover, synthase; thiolase; benzoyl-CoA. sequence analyses indicate that the residues responsible for the functional diversification of type III PKSs are mutated in benzoic acid-specific type III PDB references: benzophenone synthase, 5uco; chalcone synthase, 5uc5; biphenyl synthase, PKSs. In order to gain a better understanding of structure–function relationships 5w8q; biphenyl synthase, complex with within the type III PKS family, the crystal structures of biphenyl synthase from benzoyl-CoA, 5wc4 Malus  domestica and benzophenone synthase from Hypericum androsaemum were compared with the structure of an archetypal type III PKS: chalcone Supporting information: this article has synthase from Malus  domestica.
    [Show full text]
  • Gmmyb176 Interactome and Regulation of Isoflavonoid Biosynthesis in Soybean
    Western University Scholarship@Western Electronic Thesis and Dissertation Repository 6-28-2017 12:00 AM GmMYB176 Interactome and Regulation of Isoflavonoid Biosynthesis in Soybean Arun Kumaran Anguraj Vadivel The University of Western Ontario Supervisor Dr. Sangeeta Dhaubhadel The University of Western Ontario Joint Supervisor Dr. Mark Bernards The University of Western Ontario Graduate Program in Biology A thesis submitted in partial fulfillment of the equirr ements for the degree in Doctor of Philosophy © Arun Kumaran Anguraj Vadivel 2017 Follow this and additional works at: https://ir.lib.uwo.ca/etd Part of the Molecular Biology Commons, and the Plant Biology Commons Recommended Citation Anguraj Vadivel, Arun Kumaran, "GmMYB176 Interactome and Regulation of Isoflavonoid Biosynthesis in Soybean" (2017). Electronic Thesis and Dissertation Repository. 4639. https://ir.lib.uwo.ca/etd/4639 This Dissertation/Thesis is brought to you for free and open access by Scholarship@Western. It has been accepted for inclusion in Electronic Thesis and Dissertation Repository by an authorized administrator of Scholarship@Western. For more information, please contact [email protected]. i Abstract MYB transcription factors are one of the largest transcription factor families characterized in plants. They are classified into four types: R1 MYB, R2R3 MYB, R3 MYB and R4 MYB. GmMYB176 is an R1MYB transcription factor that regulates Chalcone synthase (CHS8) gene expression and isoflavonoid biosynthesis in soybean. Silencing of GmMYB176 suppressed the expression of the GmCHS8 gene and reduced the accumulation of isoflavonoids in soybean hairy roots. However, overexpression of GmMYB176 does not alter either GmCHS8 gene expression or isoflavonoid levels suggesting that GmMYB176 alone is not sufficient for GmCHS8 gene regulation.
    [Show full text]
  • Table 4. V. Cholerae Flexgene ORF Collection
    Table 4. V. cholerae FLEXGene ORF collection Reference Clone protein PlasmID clone GenBank Locus tag Symbol accession identifier FLEX clone name accession Product name VC0001 NP_062585 VcCD00019918 FLH200476.01F DQ772770 hypothetical protein VC0002 mioC NP_062586 VcCD00019938 FLH200506.01F DQ772771 mioC protein VC0003 thdF NP_062587 VcCD00019958 FLH200531.01F DQ772772 thiophene and furan oxidation protein ThdF VC0004 yidC NP_062588 VcCD00019970 FLH200545.01F DQ772773 inner membrane protein, 60 kDa VC0005 NP_062589 VcCD00061243 FLH236482.01F DQ899316 conserved hypothetical protein VC0006 rnpA NP_062590 VcCD00025697 FLH214799.01F DQ772774 ribonuclease P protein component VC0007 rpmH NP_062591 VcCD00061229 FLH236450.01F DQ899317 ribosomal protein L34 VC0008 NP_062592 VcCD00019917 FLH200475.01F DQ772775 amino acid ABC transporter, ATP-binding protein VC0009 NP_062593 VcCD00019966 FLH200540.01F DQ772776 amino acid ABC transproter, permease protein VC0010 NP_062594 VcCD00019152 FLH199275.01F DQ772777 amino acid ABC transporter, periplasmic amino acid-binding portion VC0011 NP_062595 VcCD00019151 FLH199274.01F DQ772778 hypothetical protein VC0012 dnaA NP_062596 VcCD00017363 FLH174286.01F DQ772779 chromosomal DNA replication initiator DnaA VC0013 dnaN NP_062597 VcCD00017316 FLH174063.01F DQ772780 DNA polymerase III, beta chain VC0014 recF NP_062598 VcCD00019182 FLH199319.01F DQ772781 recF protein VC0015 gyrB NP_062599 VcCD00025458 FLH174642.01F DQ772782 DNA gyrase, subunit B VC0016 NP_229675 VcCD00019198 FLH199346.01F DQ772783 hypothetical protein
    [Show full text]
  • Biphenyl Synthase from Gentian and Pear
    Biphenyl Synthase from Gentian and Pear Von der Fakultät für Lebenswissenschaften der Technischen Universität Carolo-Wilhelmina zu Braunschweig zur Erlangung des Grades einer Doktorin der Naturwissenschaften (Dr. rer. nat.) genehmigte Dissertation Von Asya Khemaj Swiddan aus Tripoli / Libyen 1. Referent: Prof. Dr. Ludger Beerhues 2. Referent: Prof. Dr. Thilo C. Fischer Eingereicht am: 12.05.2010 mündliche Prüfung (Disputation) am: 08.07.2010 Druckjahr 2010 Vorveröffentlichungen der Dissertation Teilergebnisse aus dieser Arbeit wurden mit Genehmigung der Fakultät für Lebenswissenschaften, vertreten durch den Mentor der Arbeit, in folgenden Beiträgen vorab veröffentlicht: Tagungsbeiträge Swiddan, K. A., Liu, B., Fischer, T.C. & Beerhues, L.: Biphenyl synthase from pear (Poster) 37. Botanikertagung: Plants for the future. Leipzig, Germany (2009). Abstract Gentiana lutea (Gentianaceae) is a herbaceous medicinal plant containing amarogentin, while pears (Pyrus sp., Rosaceae) are important fruit trees and cultivated in all temperate-zone countries. Despite their high economic value, their disease resistance mechanisms are poorly understood. Following fungal infection, biphenyls and dibenzofurans are formed as phytoalexins. Biphenylcarboxylate synthase (BICS) from gentian and biphenyl synthase (BIS) from pear are related plant-specific PKSs that are the key enzymes of the biosynthetic pathways of amarogentin and Maloideae-specific phytoalexins, respectively. Two cDNA fragments were obtained from G. lutea. The clones were 1343 and 741 bp long and shared 60.8, 51.8 % identity, respectively with chalcone synthase (Ms, CHS) but lacked appreciable identity with BIS and benzophenone synthase (BPS). In addition, two BIS cDNAs cloned from young leaves of P. communis were functionally characterized. Both enzymes preferred benzoyl-CoA (Km 1.6 for BIS1 and 1.7 for BIS2).
    [Show full text]
  • Engineering of the Aromatic Amino Acid Biosynthetic Pathways In
    ENGINEERING OF THE AROMATIC AMINO ACID BIOSYNTHETIC PATHWAYS IN ESCHERICHIA COLI FOR THE PRODUCTION OF VALUE-ADDED CHEMICALS by YUHENG LIN (Under the Direction of YAJUN YAN) ABSTRACT Aromatic amino acids (AAAs) L-phenylalanine, L-tyrosine and L-tryptophan serve not only as the building blocks for protein synthesis, but also as the precursors of secondary metabolites in organisms. A number of AAA-derived metabolites have shown pharmaceutical or industrial importance. However, these molecules usually occur in nature at low abundance, which greatly limits their efficient isolation, production and broad applications. In past decades, the development of metabolic engineering and synthetic biology facilitated the construction of ‘microbial chemical factories’ that convert renewable carbon sources to various valuable molecules. This dissertation focuses on the engineering of the E. coli AAA biosynthetic pathways to achieve the heterologous production of pharmaceutically and industrially important chemicals derived from AAAs or its biosynthetic intermediates. After careful evaluation, we select several important target compounds, including caffeic acid, simple coumarins, salicylic acid, muconic acid and 5-hydroxytryptophan and explore their production in E. coli. For this purpose, we designed, reconstituted and optimized their respective artificial biosynthetic pathways, and also conducted the modification of the E. coli native shikimate pathway via combinatorial metabolic engineering approaches. This research established powerful microbial platforms
    [Show full text]
  • Structural Diversity of Secondary Metabolites in Garcinia Species
    JNTBGRI Diversity of Garcinia species in the Western Ghats: Phytochemical Perspective Chapter 2 Structural diversity of secondary metabolites in Garcinia species A. P. Anu Aravind, Lekshmi N. Menon and K. B. Rameshkumar* Phytochemistry and Phytopharmacology Division Jawaharlal Nehru Tropical Botanic Garden and Research Institute Palode, Thiruvananthapuram-695562, Kerala, India * Corresponding author Abstract Plants of the genus Garcinia produce structurally diverse secondary metabolites such as biflavonoids, xanthones, benzophenones, flavonoids, biphenyls, acyl phloroglucinols, depsidones and terpenoids. The rich diversity in chemical structures made the genus Garcinia attractive for the phytochemists. In addition, several industrial sectors such as cosmetic, food, pharmaceutics, neutraceutics and paints are centered around the genus. The genus is represented by more than 250 species, among which nearly 120 species were subjected to phytochemical investigation. A review of the structural diversity of secondary metabolites of Garcinia species revealed that xanthones are the important class of secondary metabolites, distributed in 74 Garcinia species, followed by benzophenones in 50 species and biflavonoids in 45 species. Biphenyls, acyl phloroglucinols, depsidones and flavonoids are some other interesting group of phenolic compounds in Garcinia species. The present chapter enlists the major phenolic compounds reported from Garcinia species. Keywords: Garcinia, Secondary metabolites, Xanthones, Biflavonoids, Benzophenones Introduction Plants
    [Show full text]
  • The Enzyme Database: New Enzymes 06/27/2006 05:11 PM
    The Enzyme Database: New Enzymes 06/27/2006 05:11 PM Home Search Enzymes by Class New/Amended Enzymes Statistics Forms Advanced Search Information Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) Proposed Changes to the Enzyme List The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC- IUBMB by Keith Tipton, Sinéad Boyce, Gerry Moss and Hal Dixon, with occasional help from other Committee members, and were put on the web by Gerry Moss. Comments and suggestions on these draft entries should be sent to Professor K.F. Tipton and Dr S. Boyce (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland) by 20 May 2006, after which, the entries will be made official and will be incorporated into the main enzyme list. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list. Many thanks to those of you who have submitted details of new enzymes or updates to existing enzymes. An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry. Contents *EC 1.1.1.262 4-hydroxythreonine-4-phosphate dehydrogenase EC 1.1.1.289 sorbose reductase EC 1.1.1.290 4-phosphoerythronate dehydogenase EC 1.1.99.19 transferred *EC 1.2.1.10 acetaldehyde dehydrogenase (acetylating) EC 1.2.1.71 succinylglutamate-semialdehyde dehydrogenase EC 1.2.1.72 erythrose-4-phosphate dehydrogenase EC 1.2.99.1 transferred *EC 1.3.99.19 quinoline-4-carboxylate 2-oxidoreductase
    [Show full text]
  • Supplemental Figures 04 12 2017
    Jung et al. 1 SUPPLEMENTAL FIGURES 2 3 Supplemental Figure 1. Clinical relevance of natural product methyltransferases (NPMTs) in brain disorders. (A) 4 Table summarizing characteristics of 11 NPMTs using data derived from the TCGA GBM and Rembrandt datasets for 5 relative expression levels and survival. In addition, published studies of the 11 NPMTs are summarized. (B) The 1 Jung et al. 6 expression levels of 10 NPMTs in glioblastoma versus non‐tumor brain are displayed in a heatmap, ranked by 7 significance and expression levels. *, p<0.05; **, p<0.01; ***, p<0.001. 8 2 Jung et al. 9 10 Supplemental Figure 2. Anatomical distribution of methyltransferase and metabolic signatures within 11 glioblastomas. The Ivy GAP dataset was downloaded and interrogated by histological structure for NNMT, NAMPT, 12 DNMT mRNA expression and selected gene expression signatures. The results are displayed on a heatmap. The 13 sample size of each histological region as indicated on the figure. 14 3 Jung et al. 15 16 Supplemental Figure 3. Altered expression of nicotinamide and nicotinate metabolism‐related enzymes in 17 glioblastoma. (A) Heatmap (fold change of expression) of whole 25 enzymes in the KEGG nicotinate and 18 nicotinamide metabolism gene set were analyzed in indicated glioblastoma expression datasets with Oncomine. 4 Jung et al. 19 Color bar intensity indicates percentile of fold change in glioblastoma relative to normal brain. (B) Nicotinamide and 20 nicotinate and methionine salvage pathways are displayed with the relative expression levels in glioblastoma 21 specimens in the TCGA GBM dataset indicated. 22 5 Jung et al. 23 24 Supplementary Figure 4.
    [Show full text]
  • Research Day 2015 Program
    _____________________________________________________________________________ BREAKTHROUGHS IN REPRODUCTION AND DEVELOPMENT · NOUVELLES AVANCÉES EN REPRODUCTION ET DÉVELOPPEMENT Research Day Centre for the Study of Reproduction (CSR) at McGill Tuesday, May 19, 2015 McGill New Residence Hall 3625 Avenue du Parc Montréal, Québec ______________________________________________________________________________ BREAKTHROUGHS IN REPRODUCTION AND DEVELOPMENT Research Day 2015 Centre for the Study of Reproduction (CSR) at McGill Tuesday, May 19, 2015 New Residence Hall, 3625, avenue du Parc, Montréal, Québec 8:00-9:00 Registration and coffee / Poster set-up 9:00-9:10 Opening remarks: Dr. Daniel Bernard 9:10-10:10 Trainee oral presentations (Chairs: Steven Jones and Océane Albert) O-01. Lundi Ly, “Lifetime Folate Deficiency and Supplementation Induces Aberrant Sperm DNA Methylation and Reproductive Health” O-02. Rohini Bose, “Ubiquitin Ligase Huwe1 Modulates Male Germ Cell Development by Regulating Meiotic Progression” O-03. Stephany El Hayek, “Oocyte-Driven Remodeling of the Follicular Microenvironment Builds the Platform for Essential Germ Line-Somatic Communication” 10:10-10:40 Dr. Thomas Duchaine, Department of Biochemistry, McGill University, “What MicroRNA-Mediated Silencing in the C. elegans Embryo Can Tell Us About Cancer” – introduced by Dr. Loydie Jerome-Majewska 10:40-11:00 Health Break / Briefing of Judges 11:00-11:45 Dr. Mellissa Mann, Departments of Obstetrics & Gynecology, and Biochemistry, Schulich School of Medicine and Dentistry, University of Western Ontario, “Developmental Regulation of the Kcnq1ot1 Imprinted Domain” – introduced by Dr. Hugh Clarke 11:45-11:55 Introductory Remarks about Clermont Endowment Fund and Lectureship: Dr. Carlos Morales 11:55-12:45 Lunch 12:45-14:10 Poster Session P-01. Gauthier Schang, “Effects of Organophosphate Flame Retardants on Leydig Cell Function” P-02.
    [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]