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Phylogenetic Screening for Possible Novel
11 M060072591U NORTH-WEST UNIVERSITY tilt• YUNIBESITI YA BOKONE•BOPHIRIMA NOOROVVE S-UNIVERSITEIT PHYLOGENETIC SCREENING FOR POSSIBLE NOVEL ANTIBIOTIC PRODUCING ACTINOMYCETES FROM RHIZOSPHERIC SOIL SAMPLES COLLECTED FROM NGAKA MODIRI MOLEMA DISTRICT IN NORTH WEST PROVINCE, SOUTH AFRICA I BY MOBOLAJI FELICIA ADEGBOYE A thesis submitted in fulfilment of the requirements for the degree of DOCTOR OF PHILOSOPHY (BIOLOGY) DEPARTMENT OF BIOLOGICAL SCIENCES FACULTY OF SCIENCE, AGRICULTURE AND TECHNOLOGY NORTH-WEST UNIVERSITY, MAFIKENG CAMPUS SOUTH AFRICA Supervisor: Professor Olubukola 0. Babalola 2014 LIBRARY o MAFIKENG CAMPUS CALL NO.: 2021 -02- 0 4 DECLARATION I, the undersigned, declare that this thesis submitted to the North-West University for the degree of Doctor of Philosophy in Biology in the Faculty of Science, Agriculture and Technology, School of Environmental and Health Sciences, and the work contained herein is my original work with exemption to the citations and that this work has not been submitted at any other University in partial or entirely for the award of any degree. Name: Mobolaji Felicia Adegboye Signature: .....~ •·· ··· ····· ·· .. ··············· ..... Date: .... ~S.. .. ....a~ ·1·· ·'.}Q~i; ... ............ .... DEDICATION This work is dedicated to Almighty God for His faithfulness over my life and for making my helpers to be many. ii ACKNOWLEDGEMENTS I would like to express my deepest thanks, gratitude and appreciation to my supervisor and mentor, Prof. Olubukola 0. Babalola for giving me the opportunity to pursue my doctoral degree under her supervision and for her encouragement, help and kind support. Her invaluable advice, suggestions, discussions and guidance were a real support to me. I acknowledge with honour and gratitude the International Foundation for Science (IFS) for research grant (F/5330-1 ), Connect Africa Scholarship Award, H3ABioNet/SANBio Scholarship and North-West University for offering me bursary/scholarship award to pursue the PhD degree. -
Synthesis and Functions of Jasmonates in Maize
plants Review Synthesis and Functions of Jasmonates in Maize Eli J. Borrego and Michael V. Kolomiets * Department of Plant Pathology and Microbiology, Texas A&M University, College Station, TX 77843, USA; [email protected] * Correspondence: [email protected]; Tel.: +1-979-458-4624 Academic Editor: Eve Syrkin Wurtele Received: 29 October 2016; Accepted: 22 November 2016; Published: 29 November 2016 Abstract: Of the over 600 oxylipins present in all plants, the phytohormone jasmonic acid (JA) remains the best understood in terms of its biosynthesis, function and signaling. Much like their eicosanoid analogues in mammalian system, evidence is growing for the role of the other oxylipins in diverse physiological processes. JA serves as the model plant oxylipin species and regulates defense and development. For several decades, the biology of JA has been characterized in a few dicot species, yet the function of JA in monocots has only recently begun to be elucidated. In this work, the synthesis and function of JA in maize is presented from the perspective of oxylipin biology. The maize genes responsible for catalyzing the reactions in the JA biosynthesis are clarified and described. Recent studies into the function of JA in maize defense against insect herbivory, pathogens and its role in growth and development are highlighted. Additionally, a list of JA-responsive genes is presented for use as biological markers for improving future investigations into JA signaling in maize. Keywords: jasmonic acid; maize; lipoxygenase; oxylipins; plant-insect interactions; plant-microbe interactions 1. Importance of Maize as a Crop and a Genetic Model Despite contributing over 50% of the annual calories for humans [1] and 34% of the production for animal feed [2], little is known about fundamental hormone biology in monocot plants compared to greater advances with dicot plants, primarily Arabidopsis. -
© 2016 Shiliang Tian
© 2016 Shiliang Tian PROTEIN ENGINEERING USING AZURIN AS THE SCAFFOLD: CAPTURING AND STUDYING NOVEL METAL-SULFENATE AND METAL-NO SPECIES BY SHILIANG TIAN DISSERTATION Submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Chemistry in the Graduate College of the University of Illinois at Urbana-Champaign, 2016 Urbana, Illinois Doctoral Committee: Professor Yi Lu, Chair Professor Thomas B. Rauchfuss Professor Wilfred A. van der Donk Assistant Professor Alison R. Fout Abstract Metalloproteins account for nearly half of all proteins in nature. Metal ions play important roles in catalyzing numerous important biological processes that necessary to sustain life on the planet, such as photosynthesis, respiration and nitrogen fixation. Much effort has been made to understand the relationship between structures and functions of metalloproteins. Although significant progresses have been made to obtain the knowledge of how metalloproteins work, the ultimate test is to use this knowledge to design new metallproteins that reproduce the structures and functions of native proteins. Protein redesign strategy is one of the most effective approaches in the design and engineering of artificial metalloenzymes. The advantage of a protein redesign strategy is that it can bypass the problem of developing a stable protein fold because many native proteins have remarkable adaptability for changes. The use of small, stable, easy-to- make, and well-characterized blue copper protein azurin as scaffold to design novel metal binding sites has been proven to be a promising way for protein redesign. Not only can its reduction potential be rationally tuned beyond the nature range via secondary coordination sphere engineering, but also the CuA and redox- active nonheme iron sites have been successfully engineered in azurin. -
Microorganisms: a Potential Source of Bioactive Molecules for Antioxidants and Antimicrobial Applications
Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 4 January 2021 doi:10.20944/preprints202101.0025.v1 Review Microorganisms: A Potential Source of Bioactive molecules for Antioxidants and Antimicrobial Applications Alka Rani 1#, Khem Chand Saini 1#, Felix Bast 1, Sanjeet Mehariya 2, Shashi Kant Bhatia 3, Roberto Lavecchia 2 and Antonio Zuorro 2,* 1 Department of Botany, School of Basic and Applied Sciences, Central University of Punjab, Bathinda, Pun- jab, India -151001; [email protected] (A.R.); [email protected] (K.C.S.); [email protected] (F.B.) 2 Department of Chemical Engineering, Materials and Environment, Sapienza University of Rome, 00184 Rome, Italy; [email protected] (R.L.) 3 Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea; [email protected] (S.K.B.) * Correspondence: [email protected] (S.M.); [email protected] (A.Z.) Abstract: Oxidative stress is an elevated intracellular level of free oxygen radicals that cause lipid peroxidation, protein denaturation, DNA hydroxylation, and apoptosis, ultimately negotiating cells viability. Antioxidants can scavenge such free radicals, thus reducing the oxidative stress and even- tually prevent cellular damage. Medicinal plants, fruits, and spices remain the prioritized sources of antioxidants and antimicrobial properties since the time immemorial, but in contrast to plants, mi- croorganisms can be grown at a faster rate under controlled conditions. They are non-toxic, non- carcinogenic, and biodegradable as compared to synthetic antioxidants. Microorganisms including actinomycetes, archaea, bacteria, protozoa, yeast, and fungi are auspicious source of vital bioactive compounds. The list comprises ample of bioactive components from microorganisms. -
(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. -
Role of Rim101p in the Ph Response in Candida Albicans Michael Weyler
Role of Rim101p in the pH response in Candida albicans Michael Weyler To cite this version: Michael Weyler. Role of Rim101p in the pH response in Candida albicans. Biomolecules [q-bio.BM]. Université Paris Sud - Paris XI, 2007. English. tel-00165802 HAL Id: tel-00165802 https://tel.archives-ouvertes.fr/tel-00165802 Submitted on 27 Jul 2007 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. UNIVERSITE PARISXI UFR SCIENTIFIQUE D’ORSAY THESE présentée par Michael Weyler pour obtenir le grade de DOCTEUR EN SCIENCES DE L’UNIVERSITE PARISXI-ORSAY LE RÔLE DE RIM101p DANS LA RÉPONSE AU pH CHEZ CANDIDA ALBICANS Soutenance prévue le 6 juillet 2007 devant le jury composé de: Pr. Dr. H. Delacroix Président Dr. J-M. Camadro Rapporteur Pr. Dr. F. M. Klis Rapporteur Dr. G. Janbon Examinateur Dr. M. Lavie-Richard Examinateur Pr. Dr. C. Gaillardin Examinateur Remerciements Tout d’abord je voudrais remercier vivement mon directeur de thèse, Prof. Claude Gaillardin, pour m’avoir permis d’effectuer ce travail au sein de son laboratoire, pour ses conseils et sa disponibilité malgré son calendrier bien remplis. Je lui remercie également pour m’avoir laissé beaucoup de liberté dans mon travail, et pour la possibilité de participer aux différents congrès au cours de ma formation de thèse. -
Mechanistic Study of Cysteine Dioxygenase, a Non-Heme
MECHANISTIC STUDY OF CYSTEINE DIOXYGENASE, A NON-HEME MONONUCLEAR IRON ENZYME by WEI LI Presented to the Faculty of the Graduate School of The University of Texas at Arlington in Partial Fulfillment of the Requirements for the Degree of DOCTOR OF PHILOSOPHY THE UNIVERSITY OF TEXAS AT ARLINGTON August 2014 Copyright © by Student Name Wei Li All Rights Reserved Acknowledgements I would like to thank Dr. Pierce for your mentoring, guidance and patience over the five years. I cannot go all the way through this without your help. Your intelligence and determination has been and will always be an example for me. I would like to thank my committee members Dr. Dias, Dr. Heo and Dr. Jonhson- Winters for the directions and invaluable advice. I also would like to thank all my lab mates, Josh, Bishnu ,Andra, Priyanka, Eleanor, you all helped me so I could finish my projects. I would like to thank the Department of Chemistry and Biochemistry for the help with my academic and career. At Last, I would like to thank my lovely wife and beautiful daughter who made my life meaningful and full of joy. July 11, 2014 iii Abstract MECHANISTIC STUDY OF CYSTEINE DIOXYGENASE A NON-HEME MONONUCLEAR IRON ENZYME Wei Li, PhD The University of Texas at Arlington, 2014 Supervising Professor: Brad Pierce Cysteine dioxygenase (CDO) is an non-heme mononuclear iron enzymes that catalyzes the O2-dependent oxidation of L-cysteine (Cys) to produce cysteine sulfinic acid (CSA). CDO controls cysteine levels in cells and is a potential drug target for some diseases such as Parkinson’s and Alzhermer’s. -
Oxylipins: Structurally Diverse Metabolites from Fatty Acid Oxidation
Plant Physiology and Biochemistry 47 (2009) 511–517 Contents lists available at ScienceDirect Plant Physiology and Biochemistry journal homepage: www.elsevier.com/locate/plaphy Review Oxylipins: Structurally diverse metabolites from fatty acid oxidation Alina Mosblech, Ivo Feussner*, Ingo Heilmann* Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, Georg-August-University Go¨ttingen, Justus-von-Liebig-Weg 11, 37077 Go¨ttingen, Germany article info abstract Article history: Oxylipins are lipophilic signaling molecules derived from the oxidation of polyunsaturated fatty acids. Received 2 October 2008 Initial fatty acid oxidation occurs mainly by the enzymatic or chemical formation of fatty acid hydro- Accepted 8 December 2008 peroxides. An array of alternative reactions further converting fatty acid hydroperoxides gives rise to Available online 25 December 2008 a multitude of oxylipin classes, many with reported signaling functions in plants. Oxylipins include the phytohormone, jasmonic acid, and a number of other molecules including hydroxy-, oxo- or keto-fatty Keywords: acids or volatile aldehydes that may perform various biological roles as second messengers, messengers Cyp74 in inter-organismic signaling, or even as bactericidal agents. The structural diversity of oxylipins is Fatty acid peroxides Lipid metabolism further increased by esterification of the compounds in plastidial glycolipids, for instance the Arabi- Lipid peroxidation dopsides, or by conjugation of oxylipins to amino acids or other metabolites. The enzymes involved in Lipid signaling oxylipin metabolism are diverse and comprise a multitude of examples with interesting and unusual Lipoxygenase pathway catalytic properties. In addition, the interplay of different subcellular compartments during oxylipin biosynthesis suggests complex mechanisms of regulation that are not well understood. -
Generate Metabolic Map Poster
Authors: Zheng Zhao, Delft University of Technology Marcel A. van den Broek, Delft University of Technology S. Aljoscha Wahl, Delft University of Technology Wilbert H. Heijne, DSM Biotechnology Center Roel A. Bovenberg, DSM Biotechnology Center Joseph J. Heijnen, Delft University of Technology An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Marco A. van den Berg, DSM Biotechnology Center Peter J.T. Verheijen, Delft University of Technology Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. PchrCyc: Penicillium rubens Wisconsin 54-1255 Cellular Overview Connections between pathways are omitted for legibility. Liang Wu, DSM Biotechnology Center Walter M. van Gulik, Delft University of Technology L-quinate phosphate a sugar a sugar a sugar a sugar multidrug multidrug a dicarboxylate phosphate a proteinogenic 2+ 2+ + met met nicotinate Mg Mg a cation a cation K + L-fucose L-fucose L-quinate L-quinate L-quinate ammonium UDP ammonium ammonium H O pro met amino acid a sugar a sugar a sugar a sugar a sugar a sugar a sugar a sugar a sugar a sugar a sugar K oxaloacetate L-carnitine L-carnitine L-carnitine 2 phosphate quinic acid brain-specific hypothetical hypothetical hypothetical hypothetical -
Downloaded from Uniprotkb/Swiss-Prot ( and Concatenated with the Reverse One
International Journal of Molecular Sciences Article Root Proteomic Analysis of Two Grapevine Rootstock Genotypes Showing Different Susceptibility to Salt Stress Bhakti Prinsi , Osvaldo Failla , Attilio Scienza and Luca Espen * Department of Agricultural and Environmental Sciences—Production, Landscape, Agroenergy (DiSAA), Università degli Studi di Milano, Via Celoria 2, 20133 Milano, Italy; [email protected] (B.P.); [email protected] (O.F.); [email protected] (A.S.) * Correspondence: [email protected]; Tel.: +39-02-503-16610 Received: 21 December 2019; Accepted: 4 February 2020; Published: 6 February 2020 Abstract: Salinity represents a very limiting factor that affects the fertility of agricultural soils. Although grapevine is moderately susceptible to salinity, both natural causes and agricultural practices could worsen the impact of this abiotic stress. A promising possibility to reduce this problem in vineyards is the use of appropriate graft combinations. The responses of grapevine rootstocks to this abiotic stress at the root level still remain poorly investigated. In order to obtain further information on the multifaceted responses induced by salt stress at the biochemical level, in the present work we analyzed the changes that occurred under control and salt conditions in the root proteomes of two grapevine rootstock genotypes, M4 and 101.14. Moreover, we compared the results considering that M4 and 101.14 were previously described to have lower and higher susceptibility to salt stress, respectively. This study highlighted the greater capability of M4 to maintain and adapt energy metabolism (i.e., synthesis of ATP and NAD(P)H) and to sustain the activation of salt-protective mechanisms (i.e., Na sequestration into the vacuole and synthesis of osmoprotectant compounds). -
The Bioinorganic Chemistry of Copper-Containing Systems: from Type-3 Systems Pertinent to Alzheimer's Disease to Mononuclear H
The Bioinorganic Chemistry Of Copper-Containing Systems: From Type-3 Systems Pertinent To Alzheimer’s Disease To Mononuclear Hydrolysis Involved In Biological Development by Giordano Faustini Zimmerer Da Silva A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy Department of Chemistry College of Arts and Sciences University of South Florida Co-Major Professor: Li-June Ming, Ph.D. Co-Major Professor: Brian T. Livingston, Ph.D. Steven H. Grossman, Ph.D. Randy L. Larsen, Ph.D. Date of Approval: May 9, 2007 Keywords: kinetics, reactive oxygen species, metallopeptide, amyloid, enzymology, sea urchin, metalloprotease © Copyright 2007 , Giordano F.Z. Da Silva NOTE TO THE READER Note to Reader: The original of this document contains color that is necessary for understanding the data. The original dissertation is on file at the USF library in Tampa, FL. DEDICATION Although the graduate school experience is highly a personal journey, it would be foolish to believe that I was solely responsible for my accomplishments. I then would like to dedicate this work to all of those who have played a major role in this difficult yet rewarding part of my life. First my grandmother Ermelinda who is the sole reason why I am in the US, my parents Mauricio and Marta for sacrificing the presence of their son, and my sister Marcella for being sibling, friend and parent through part of my formative years. Second I must dedicate this work to the Kelley family for being my parents, brother, and sisters; Moms, Pops, John, Tere, and Abbie, I would not be here today without your love and support. -
12) United States Patent (10
US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S.