DOCSLIB.ORG

Gmmyb176 Interactome and Regulation of Isoflavonoid Biosynthesis in Soybean

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read 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. I hypothesized that GmMYB176 acts cooperatively with another factor(s) for the regulation of GmCHS8 gene expression and it may also regulate other isoflavonoid biosynthetic genes in soybean. The objective of this research was to identify the GmMYB176 interactome for GmCHS8 gene regulation and elucidate the role of GmMYB176 in isoflavonoid biosynthesis in soybean. GmMYB176 interacting proteins were identified using two translational fusion baits (GmMYB176-YFP and YFP-GmMYB176) by co-immunoprecipitation, followed by liquid chromatography-tandem mass spectrometry. The interaction of selected candidates with GmMYB176 was validated in planta and their DNA binding activities determined. GmMYB176 may form a transcriptional complex with Gm04bZIP and/or Gm05bZIP for the regulation of GmCHS8 gene expression. RNA-seq and metabolomics analyses of soybean hairy roots in which GmMYB176 was either silenced or over-expressed revealed that GmMYB176 regulates multiple genes in the isoflavonoid biosynthesis pathway, affecting the production of metabolites in phenylpropanoid pathway such as phenylalanine, liquiritigenin, daidzin, genistin, glycitein, and glyceollin. The knowledge and information generated on the role of GmMYB176 in the regulation of isoflavonoid biosynthesis will allow genetic manipulation of isoflavonoid level in soybean and/or introduce isoflavonoid pathway in non-legumes. Keywords Co-immunoprecipitation, LC-MS/MS, MYB, protein-protein interaction, transcriptomics, metabolomics, isoflavonoid, phenylpropanoid, secondary metabolism, transcriptional complex, gene regulation, gene families, soybean ii Acknowledgements I dedicate this thesis to my non-biological father, Mr. N. Thangavel. Thanks as well to my parents Mr. Anguraj Vadivel and Mrs. Thilagavathy, my sister, Mrs. Priyadharshini for their support in me pursue a research in Canada, far away from home. I also thank my cousins Ms. Kamalapriya and Mr. Suryakumar for their support. I would like to thank my adopted family at Agriculture and Agri-Food Canada (AAFC), London. Everyone in the Dhaubhadel lab (past and present), Mehran, Hemanta, Kishor, Pravesh, Arjun, Caroline, Xuyan, Shaomin, Serina, Amelia, Jaeju, Kevin, Kelsey, Smarth, and Nishat – thank you for your support and encouragement. I would also like to thank Ling, for her lab technical advice and life advice. Moreover, I would like to thank all my friends in other labs (in AAFC) FM lab, CD lab, IS lab, AH lab, RM lab, RA lab, YC lab (and so many) for lighting up my days and for all those memories in last five years. I also thank my friends, Aagam, Milan, Preetam and Rohan from dept of chemistry, biochemistry, and geology. I must thank the individuals who have been essential to the present research: my advisory committee, Dr. Jim Karagiannis and Dr. Frederic Marsolais for their input and guidance; I also thank my co-supervisor, Dr. Mark Bernards for his insights and his invaluable advice for my research and in general. I would like to thank Dr. Justin Renaud for his help in analyzing metabolite samples and teaching me a lot about metabolomics. I also thank London Regional Proteomics Center, UWO for their help in analyzing my protein samples. Most importantly, I must thank my supervisor, Dr. Sangeeta Dhaubhadel for giving me the opportunity to join her lab and for her guidance, support, and encouragement in science. iii Table of Contents Abstract ................................................................................................................................. i Acknowledgements ............................................................................................................ ii Table of Contents .............................................................................................................. iii List of Tables .................................................................................................................... vii List of Figures .................................................................................................................. viii List of Appendices ............................................................................................................... x List of Abbreviations .......................................................................................................... xi 1 GENERAL INTRODUCTION ...................................................................................... 1 1.1 Soybean ................................................................................................................... 1 1.1.1 Soybean genome .......................................................................................... 1 1.2 Phenylpropanoid pathway ....................................................................................... 2 1.3 Isoflavonoids ........................................................................................................... 2 1.3.1 Role of isoflavonoids in human health and nutrition .................................. 4 1.3.2 Role of isoflavonoids in plants .................................................................... 4 1.4 Isoflavonoid biosynthesis in soybean ...................................................................... 5 1.4.1 Overview of the pathway ............................................................................. 5 1.4.2 Regulation and accumulation of isoflavonoids in soybean tissues ............. 9 1.5 MYB transcription factors and transcriptional complexes .................................... 11 1.6 GmMYB176: the regulator of isoflavonoid biosynthesis in soybean ................... 14 1.7 Objectives of the study .......................................................................................... 17 1.8 Literature cited ....................................................................................................... 18 2 IDENTIFICATION OF SOYBEAN CHS GENE FAMILY MEMBERS ................... 28 2.1 Introduction ........................................................................................................... 28 2.2 Materials and methods ........................................................................................... 30 iv 2.2.1 In silico and phylogenetic analysis ............................................................ 30 2.2.2 Generation of a heat map ........................................................................... 30 2.3 Results ................................................................................................................... 31 2.3.1 The GmCHS family contains 14 putative members .................................. 31 2.3.2 GmCHS transcript accumulation vary in soybean tissues ......................... 32 2.4 Discussion .............................................................................................................. 40 2.4.1 Soybean genome contains 14 putative GmCHS genes .............................. 40 2.4.2 GmCHSs display tissue-specific expression in soybean............................ 42 2.5 Conclusion ............................................................................................................. 43 2.6 Literature cited ....................................................................................................... 44 3 GmMYB176 INTERACTOME: KEY FACTORS IN ISOFLAVONOID BIOSYNTHESIS IN SOYBEAN .............................................................................................................. 47 3.1 Introduction ........................................................................................................... 47 3.2 Materials and methods ........................................................................................... 49 3.2.1 Plant
Load more

Recommended publications
  • Olarewaju Olaoluwa Omoniyi 2
    EFFECT OF CANOPY POSITION AND NON-DESTRUCTIVE DETERMINATION OF RIND BIOCHEMICAL PROPERTIES OF CITRUS FRUIT DURING POSTHARVEST NON-CHILLING COLD STORAGE OLAOLUWA OMONIYI OLAREWAJU Submitted in partial fulfilment of the academic requirements for the degree of DOCTOR OF PHILOSOPHY Discipline of Horticultural Science School of Agricultural, Earth and Environmental Sciences College of Agriculture, Engineering, and Sciences University of KwaZulu-Natal Pietermaritzburg South Africa December 2017 FOREWORD The research contained in this thesis was completed by the candidate while based in the Discipline of Horticultural Sciences, School of Agricultural, Earth and Environmental Sciences of the College of Agriculture, Engineering and Science, University of KwaZulu-Natal, Pietermaritzburg, South Africa. The research was made possible by the funding received from National Research Foundation and Citrus Research International through Postharvest Innovation Programme (PHI 2/2014). The contents of this work have not been submitted in any form to another university and, except where the work of others is acknowledged in the text, the results reported are due to investigations by the candidate. _________________________ _________________________ Signed: Dr LS Magwaza Signed: Dr OA Fawole Date: Date: _________________________ _________________________ Signed: Dr SZ Tesfay Signed: Prof UL Opara Date: Date: i DECLARATION 1- PLAGIARISM I, Olarewaju Olaoluwa Omoniyi, declare that: 1) The research reported in this dissertation, except where otherwise indicated or acknowledged, is my original work; 2) This dissertation has not been submitted in full or in part for any degree or examination to any other university; 3) This dissertation does not contain other persons’ data, pictures, graphs, or other information, unless specifically acknowledged as being sourced from other persons; 4) This dissertation does not contain other persons’ writing, unless specifically acknowledged as being sourced from other researchers.
    [Show full text]
  • 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]
  • Chloroplasts and Plant Immunity: Where Are the Fungal Effectors?
    pathogens Review Chloroplasts and Plant Immunity: Where Are the Fungal Effectors? Matthias Kretschmer 1, Djihane Damoo 1, Armin Djamei 2 and James Kronstad 1,* 1 Michael Smith Laboratories, Department of Microbiology and Immunology, University of British Columbia, Vancouver, BC V6T 1Z4, Canada; [email protected] (M.K.); [email protected] (D.D.) 2 Leibniz Institute of Plant Genetics and Crop Plant Research (IPK) OT Gatersleben Corrensstrasse 3, D-06466 Stadt Seeland, Germany; [email protected] * Correspondence: [email protected]; Tel.: +604-822-4732 Received: 4 December 2019; Accepted: 21 December 2019; Published: 24 December 2019 Abstract: Chloroplasts play a central role in plant immunity through the synthesis of secondary metabolites and defense compounds, as well as phytohormones, such as jasmonic acid and salicylic acid. Additionally, chloroplast metabolism results in the production of reactive oxygen species and nitric oxide as defense molecules. The impact of viral and bacterial infections on plastids and chloroplasts has been well documented. In particular, bacterial pathogens are known to introduce effectors specifically into chloroplasts, and many viral proteins interact with chloroplast proteins to influence viral replication and movement, and plant defense. By contrast, clear examples are just now emerging for chloroplast-targeted effectors from fungal and oomycete pathogens. In this review, we first present a brief overview of chloroplast contributions to plant defense and then discuss examples of connections between fungal interactions with plants and chloroplast function. We then briefly consider well-characterized bacterial effectors that target chloroplasts as a prelude to discussing the evidence for fungal effectors that impact chloroplast activities.
    [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]
  • Functional Characterization of Prenyltransferases Involved in the Biosynthesis of Polycyclic Polyprenylated Acylphloroglucinols in the Genus Hypericum
    Functional characterization of prenyltransferases involved in the biosynthesis of polycyclic polyprenylated acylphloroglucinols in the genus Hypericum Von der Fakultät für Lebenswissenschaften der Technischen Universität Carolo-Wilhelmina zu Braunschweig zur Erlangung des Grades eines Doktors der Naturwissenschaften (Dr. rer. nat.) genehmigte D i s s e r t a t i o n von Mohamed Mamdouh Sayed Nagia aus Kalyobiya/ Ägypten 1. Referent: Professor Dr. Ludger Beerhues 2. Referent: Professor Dr. Alain Tissier eingereicht am: 30.07.2018 mündliche Prüfung (Disputation) am: 15.10.2018 Druckjahr 2018 „Gedruckt mit Unterstützung des Deutschen Akademischen Austauschdienstes“ „Und sag: O mein Herr, mehre mein Wissen“ Der Edle Qur’an [20: 114] 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: Publikationen Nagia, M., Gaid, M., Biedermann, E., Fiesel, T., El-Awaad, I., Haensch, R., Wittstock, U., and Beerhues, L. Sequential regiospecific gem-diprenylation of tetrahydroxyxanthone by prenyltransferases from Hypericum sp. (Submitted). Nagia, M., Gaid, M., Beuerle, T., and Beerhues, L. Successive xanthone prenylation in Hypericum sampsonii. Planta Medica International Open 4, Tu-SL-01 (2017). doi: 10.1055/s-0037-1608308 Tagungsbeiträge A. Vorträge Nagia M., Gaid M., Biedermann E., Beuerle T., Beerhues L., Successive xanthone prenylation in Hypericum sampsonii, 65th Annual Meeting of the Society for Medicinal Plant and Natural Product Research, Basel, Switzerland, 3. – 7. September 2017. Nagia M., Gaid M., Behrends S., Beerhues L., Novel PPAP-related prenyltransferases, 4. SynFoBiA -Kolloquium des Pharmaverfahrenstechnik (PVZ), Braunschweig, Germany, 26. February 2016. Nagia M., Gaid M., Beurele T., Biedermann E., Beerhues L., Aromatic Prenyltransferases from Hypericum sampsonii, Postgraduate workshop of the section „Natural Products“ German Society for Plant Sciences (DBG), Meisdorf, Germany , 11.
    [Show full text]
  • Machovina-Enzymatic-2018.Pdf
    ENZYMATIC STRATEGIES FOR CONTROLLING AND HARNESSING THE OXIDATIVE POWER OF O2 by Melodie M. Machovina A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biochemistry MONTANA STATE UNIVERSITY Bozeman, Montana November 2018 ©COPYRIGHT by Melodie Marie Machovina 2018 All Rights Reserved ii DEDICATION I would like to dedicate this work to my parents, Alberto and Gina, whose outstanding dedication to excellence and hard-work has encouraged me to persevere through all that life has given. This dissertation is also dedicated to my godfather, Murray Oxman, a true friend and inspiration. Your wisdom has guided me along this journey and continues to guide me! iii ACKNOWLEDGMENTS My first and foremost thanks go to my advisor, Prof. Jennifer DuBois; your passion and dedication towards excellent science is an inspiration. Thank you for your guidance along this significant chapter in my life! I would also like to acknowledge my thesis committee members, Profs. Joan Broderick, Valerie Copie, and Brian Bothner, and Dr. Gregg Beckham for all that you’ve taught me along the way. I am grateful to my collaborators for providing excellent data and being great to work with. A special thanks to Gregg Beckham for taking me under his wing at NREL and always being so excited and positive. I would also like to acknowledge John McGeehan and Sam Mallinson in the UK; it’s been a pleasure working with you on the amazing GcoA stories. Thank you for making our collaboration so enjoyable and productive! Doreen Brown, thank you for helping make grad school a smooth and enjoyable experience.
    [Show full text]
  • (10) Patent No.: US 8119385 B2
    US008119385B2 (12) United States Patent (10) Patent No.: US 8,119,385 B2 Mathur et al. (45) Date of Patent: Feb. 21, 2012 (54) NUCLEICACIDS AND PROTEINS AND (52) U.S. Cl. ........................................ 435/212:530/350 METHODS FOR MAKING AND USING THEMI (58) Field of Classification Search ........................ None (75) Inventors: Eric J. Mathur, San Diego, CA (US); See application file for complete search history. Cathy Chang, San Diego, CA (US) (56) References Cited (73) Assignee: BP Corporation North America Inc., Houston, TX (US) OTHER PUBLICATIONS c Mount, Bioinformatics, Cold Spring Harbor Press, Cold Spring Har (*) Notice: Subject to any disclaimer, the term of this bor New York, 2001, pp. 382-393.* patent is extended or adjusted under 35 Spencer et al., “Whole-Genome Sequence Variation among Multiple U.S.C. 154(b) by 689 days. Isolates of Pseudomonas aeruginosa” J. Bacteriol. (2003) 185: 1316 1325. (21) Appl. No.: 11/817,403 Database Sequence GenBank Accession No. BZ569932 Dec. 17. 1-1. 2002. (22) PCT Fled: Mar. 3, 2006 Omiecinski et al., “Epoxide Hydrolase-Polymorphism and role in (86). PCT No.: PCT/US2OO6/OOT642 toxicology” Toxicol. Lett. (2000) 1.12: 365-370. S371 (c)(1), * cited by examiner (2), (4) Date: May 7, 2008 Primary Examiner — James Martinell (87) PCT Pub. No.: WO2006/096527 (74) Attorney, Agent, or Firm — Kalim S. Fuzail PCT Pub. Date: Sep. 14, 2006 (57) ABSTRACT (65) Prior Publication Data The invention provides polypeptides, including enzymes, structural proteins and binding proteins, polynucleotides US 201O/OO11456A1 Jan. 14, 2010 encoding these polypeptides, and methods of making and using these polynucleotides and polypeptides.
    [Show full text]
  • Scientific Report | 2016/2017
    Research Area Center for Molecular Biosciences (CMBI) scientific report | 2016/2017 Scientific Coordinators Bert Hobmayer, Ronald Micura, Jörg Striessnig 2 Imprint 3 The Research Area Center for Molecular Biosciences Innsbruck (CMBI) – a life science network in western Austria In our biannual report, the Center for Molecular Biosciences of Innsbruck University (CMBI) presents its recent scientific achievements, new developments in ongoing research projects and success stories of its faculty members, especially of young researchers. Molecular biosciences represent one of the most exciting fields of modern research among the natural sciences. They bridge the gap between single molecules and the complex functions in living organisms under normal conditions and in disease. Minor changes in bioactive molecules such as DNA, RNA and proteins affect and change the properties of cells, microorganisms, animals and plants. Advances in technologies including microscopic imaging, new generation sequencing applications and techniques to analyze molecular structures result in an explosion of information and understanding of biological systems primarily oriented to improve human health. The CMBI aims at providing a platform for this extremely rapidly developing research field by taking advantage of the visibility and expertise of the CMBI’s internationally competitive groups to strengthen interdisciplinary research activities. The CMBI currently consists of 21 research teams originating from the faculties of Chemistry and Pharmacy, of Biology, and of Mathematics, Informatics and Physics, and their activities focus on research and teaching. CMBI members contribute to the FWF special research program SFB-F44 “Cell Signaling in Chronic CNS Disorders”, which is currently in its second funding period, and to several FWF-funded doctoral programs, all in collaboration with the Medical University of Innsbruck.
    [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]
  • Molecular Analysis of Coenzyme a Ligase from Benzoate-Metabolizing Sorbus Aucuparia Cell Cultures
    Molecular analysis of coenzyme A ligase from benzoate-metabolizing Sorbus aucuparia cell cultures Von der Fakultät für Lebenswissenschaften der Technischen Universität Carolo-Wilhelmina zu Braunschweig zur Erlangung des Grades eines Doktors der Naturwissenschaften (Dr. rer. nat) genehmigte D i s s e r t a t i o n von Hussein Ramadan aus Rabta, Libyen 1. Referee: Prof. Dr. Ludger Beerhues 2. Referee: apl. Prof. Dr. Dirk Selmar eingereicht am: 14.08.2006 mündliche Prüfung (Disputation) am: 19.10.2006 Druckjahr : 2006 Parts of this work have previously been published with permission of the Faculty of Life Science, represented by the mentor of this work: Presentations -Short lecture Ramadan, H , Beerhues, L (2005) Coenzyme A ligases involved in benzoic acid biosynthesis XVII International Botanical Congress Austria Center Vienna, 17 - 23 July 2005 -Poster Ramadan, H , Beerhues, L (2004) Coenzyme A ligases involved in benzoic acid biosynthesis Botanikertagung der Deutschen Botanischen Gesellschaft und der Vereinigung für Angewandte Botanik Braunschweig, 05-10 September 2004 ACKNOWLEDGEMENTS I would like to express my gratitude to many individuals who assisted me throughout the course of my doctoral research. First and foremost, I would like to express my gratitude to my advisor, Professor Dr. Ludger Beerhues, for the wonderful opportunity of participating in this exciting research endeavour and for constant guidance, unwavering moral support during my years as PhD student. More thanks for his patience to correct from the beginning to the end my thesis tirelessly, and for the extraordinary advice, caring, encouragement, and affection he bestowed on me. My sincere thanks go to Prof. Dr.
    [Show full text]
  • The Science of Flavonoids the Science of Flavonoids
    The Science of Flavonoids The Science of Flavonoids Edited by Erich Grotewold The Ohio State University Columbus, Ohio, USA Erich Grotewold Department of Cellular and Molecular Biology The Ohio State University Columbus, Ohio 43210 USA [email protected] The background of the cover corresponds to the accumulation of flavonols in the plasmodesmata of Arabidopsis root cells, as visualized with DBPA (provided by Dr. Wendy Peer). The structure corresponds to a model of the Arabidopsis F3 'H enzyme (provided by Dr. Brenda Winkel). The chemical structure corresponds to dihydrokaempferol. Library of Congress Control Number: 2005934296 ISBN-10: 0-387-28821-X ISBN-13: 978-0387-28821-5 ᭧2006 Springer ScienceϩBusiness Media, Inc. All rights reserved. This work may not be translated or copied in whole or in part without the written permission of the publisher (Springer ScienceϩBusiness Media, Inc., 233 Spring Street, New York, NY 10013, USA), except for brief excerpts in connection with reviews or scholarly analysis. Use in connection with any form of information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed is forbidden. The use in this publication of trade names, trademarks, service marks and similar terms, even if they are not identified as such, is not to be taken as an expression of opinion as to whether or not they are subject to proprietary rights. Printed in the United States of America (BS/DH) 987654321 springeronline.com PREFACE There is no doubt that among the large number of natural products of plant origin, debatably called secondary metabolites because their importance to the eco- physiology of the organisms that accumulate them was not initially recognized, flavonoids play a central role.
    [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]