Dictionary of DNA and Genome Technology, Second Edition
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Babela Massiliensis, a Representative of a Widespread Bacterial
Babela massiliensis, a representative of a widespread bacterial phylum with unusual adaptations to parasitism in amoebae Isabelle Pagnier, Natalya Yutin, Olivier Croce, Kira S Makarova, Yuri I Wolf, Samia Benamar, Didier Raoult, Eugene V. Koonin, Bernard La Scola To cite this version: Isabelle Pagnier, Natalya Yutin, Olivier Croce, Kira S Makarova, Yuri I Wolf, et al.. Babela mas- siliensis, a representative of a widespread bacterial phylum with unusual adaptations to parasitism in amoebae. Biology Direct, BioMed Central, 2015, 10 (13), 10.1186/s13062-015-0043-z. hal-01217089 HAL Id: hal-01217089 https://hal-amu.archives-ouvertes.fr/hal-01217089 Submitted on 19 Oct 2015 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. Pagnier et al. Biology Direct (2015) 10:13 DOI 10.1186/s13062-015-0043-z RESEARCH Open Access Babela massiliensis, a representative of a widespread bacterial phylum with unusual adaptations to parasitism in amoebae Isabelle Pagnier1, Natalya Yutin2, Olivier Croce1, Kira S Makarova2, Yuri I Wolf2, Samia Benamar1, Didier Raoult1, Eugene V Koonin2 and Bernard La Scola1* Abstract Background: Only a small fraction of bacteria and archaea that are identifiable by metagenomics can be grown on standard media. -
Genetic Snapshots of the Rhizobium Species NGR234 Genome
Article Genetic snapshots of the Rhizobium species NGR234 genome VIPREY, Virginie, et al. Abstract In nitrate-poor soils, many leguminous plants form nitrogen-fixing symbioses with members of the bacterial family Rhizobiaceae. We selected Rhizobium sp. NGR234 for its exceptionally broad host range, which includes more than I 12 genera of legumes. Unlike the genome of Bradyrhizobium japonicum, which is composed of a single 8.7 Mb chromosome, that of NGR234 is partitioned into three replicons: a chromosome of about 3.5 Mb, a megaplasmid of more than 2 Mb (pNGR234b) and pNGR234a, a 536,165 bp plasmid that carries most of the genes required for symbioses with legumes. Symbiotic loci represent only a small portion of all the genes coded by rhizobial genomes, however. To rapidly characterize the two largest replicons of NGR234, the genome of strain ANU265 (a derivative strain cured of pNGR234a) was analyzed by shotgun sequencing. Reference VIPREY, Virginie, et al. Genetic snapshots of the Rhizobium species NGR234 genome. Genome Biology, 2000, vol. 1, no. 6, p. 1-17 DOI : 10.1186/gb-2000-1-6-research0014 PMID : 11178268 Available at: http://archive-ouverte.unige.ch/unige:84778 Disclaimer: layout of this document may differ from the published version. 1 / 1 http://genomebiology.com/2000/1/6/research/0014.1 Research Genetic snapshots of the Rhizobium species NGR234 genome Virginie Viprey*, André Rosenthal, William J Broughton* and Xavier Perret* Addresses: *Laboratoire de Biologie Moléculaire des Plantes Supérieures, Université de Genève, chemin de lImpératrice, 1292 Chambésy, Genève, Switzerland. Institut für Molekulare Biotechnologie, Abteilung Genomanalyze, Beutenbergstrasse, 07745 Jena, Germany. -
2.2.3 Generation of Genomic DNA Sequences from Plant Sources
Copyright Undertaking This thesis is protected by copyright, with all rights reserved. By reading and using the thesis, the reader understands and agrees to the following terms: 1. The reader will abide by the rules and legal ordinances governing copyright regarding the use of the thesis. 2. The reader will use the thesis for the purpose of research or private study only and not for distribution or further reproduction or any other purpose. 3. The reader agrees to indemnify and hold the University harmless from and against any loss, damage, cost, liability or expenses arising from copyright infringement or unauthorized usage. IMPORTANT If you have reasons to believe that any materials in this thesis are deemed not suitable to be distributed in this form, or a copyright owner having difficulty with the material being included in our database, please contact [email protected] providing details. The Library will look into your claim and consider taking remedial action upon receipt of the written requests. Pao Yue-kong Library, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong http://www.lib.polyu.edu.hk The Hong Kong Polytechnic University Department of Health Technology and Informatics Isolation and Characterisation of Nucleases from Various Biological Sources for Further Application in Nucleic Acid Analysis By CHEUNG Tsz Shan A thesis submitted in partial fulfilment of the requirements for the degree of Doctor of Philosophy March 2012 CERTIFICATE OF ORIGINALITY I hereby declare that this thesis is my own work and that, to the best of my knowledge and belief, it reproduces no materials previously published or written, nor material that has been accepted for the award of any other degree or diploma, except where due acknowledgment has been made in the text. -
Mung Bean Nuclease Product Information
Certificate of Analysis Mung Bean Nuclease: Part No. Size (units) Part# 9PIM431 M431A 2,000 Revised 4/18 10X Reaction Buffer (M432A): When the Mung Bean Nuclease 10X Reaction Buffer, provided with this enzyme, is diluted 1:10, it has a composition of 0.03M sodium acetate (pH 5.0), 0.05M NaCl and 1mM ZnCl2. Enzyme Storage Buffer: Mung Bean Nuclease is supplied in 10mM Tris-HCl (pH 7.5), 50mM NaCl, 0.01% Triton® X-100 and 50% glycerol. Source: Mung bean sprouts (Phaseolus aureus). Unit Definition: One unit is defined as the amount of enzyme required to produce 1µg of acid-soluble material per minute *AF9PIM431 0418M431* at 37°C. The reaction conditions are: 30mM sodium acetate (pH 5.0), 50mM NaCl, 1mM ZnCl2, 5% glycerol and 0.5mg/ml AF9PIM431 0418M431 denatured calf thymus DNA. See the unit concentration on the Product Information Label. Storage Temperature: Store at –20°C. Avoid multiple freeze-thaw cycles and exposure to frequent temperature changes. See the expiration date on the Product Information Label. Quality Control Assays Contaminant Assay Endonuclease/Nickase Activity: To confirm the absence of contaminating endonuclease/nickase activity, 1µg of lambda DNA/Hind III markers (Cat.# G1711) is incubated with Mung Bean Nuclease for 10 minutes at room temperature. The mark- ers are then separated by electrophoresis on a 1% agarose gel and stained with ethidium bromide. Markers that have been Promega Corporation incubated with ≥60 units of enzyme will remain as intact bands with a minimal amount of smearing. 2800 Woods Hollow Road Madison, WI 53711-5399 USA Telephone 608-274-4330 Toll Free 800-356-9526 Fax 608-277-2516 Internet www.promega.com PRODUCT USE LIMITATIONS, WARRANTY, DISCLAIMER Promega manufactures products for a number of intended uses. -
O-Alkyl Oligoribonucleotides As Antisense Probes (Modified RNA/Afnity Selection/Ribonudeoprotein Couiplexes/Oligonucleotide Synthesis/Biotinylation) ADOLFO M
Proc. Nail. Acad. Sci. USA Vol. 87, pp, 7747-7751, October 1990 Biochemistry 2'-O-Alkyl oligoribonucleotides as antisense probes (modified RNA/afnity selection/ribonudeoprotein couiplexes/oligonucleotide synthesis/biotinylation) ADOLFO M. IRIBARREN*, BRIAN S. SPROAT, PHILIPPE NEUNER*, INGRID SULSTON, URSULA RYDER, AND ANGUS 1. LAMOND European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 102209, D6900 Heidelberg 1, Federal Republic of Germany Communicated by J. A. Steitz, July 3, 1990 (receivedfor review May 1, 1990) ABSTRACT 2'-O-Methyl oligoribonucleotides have re- cently been introduced as antisense probes for studying RNA processing and for affinity purification of RNA-protein com- plexes. To identify RNA analogues with improved properties for antisense analysis, 2'--alkyl oligoribonucleotides were synthesized in which the alkyl moiety was either the three- carbon linear allyl group or the five-carbon branched 3,3- dimethylallyl group. Both these analogues were found to be completely resistant to degradation by either DNA- or RNA- specific nucleases. Use of biotinylated derivatives of the probes to affinity-select ribonucleoprotein particles from crude HeLa cell nuclear extracts showed that the presence of the bulky L i3 3,3-dimethylallyl group significantly reduces affinity selection, -o'r\- .. whereas the allyl derivative binds rapidly and stably to targeted sequences and affinity-selects efficiently. The allyl derivatives also showed an increase in the level of specific binding to targeted sequences compared with 2'-0-methyl probes of iden- tical sequence. These properties indicate that the 2'-0-allyl oligoribonucleotides are particularly well suited for use as HO OR antisense probes. S H Chemically synthesized 2'-O-methyl oligoribonucleotides, as R NH described by Ohtsuka and Morisawa and coworkers (1-6) and by Sproat et al. -
WO 2013/185113 Al 12 December 2013 (12.12.2013) P O P C T
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2013/185113 Al 12 December 2013 (12.12.2013) P O P C T (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every A61K 38/02 (2006.01) A61P 7/02 (2006.01) kind of national protection available): AE, AG, AL, AM, A61K 38/36 (2006.01) AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, (21) Number: International Application DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, PCT/US20 13/044841 HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KN, KP, KR, (22) International Filing Date: KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, 7 June 2013 (07.06.2013) MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SC, (25) Filing Language: English SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, (26) Publication Language: English TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (30) Priority Data: (84) Designated States (unless otherwise indicated, for every 61/657,688 8 June 2012 (08.06.2012) kind of regional protection available): ARIPO (BW, GH, 61/800,626 15 March 2013 (15.03.2013) GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, (71) Applicant: BIOGEN IDEC MA INC. -
Next Generation Sequencing Identifies Five Major Classes of Potentially Therapeutic Enzymes Secreted by Lucilia Sericata Medical Maggots
Hindawi Publishing Corporation BioMed Research International Volume 2016, Article ID 8285428, 27 pages http://dx.doi.org/10.1155/2016/8285428 Research Article Next Generation Sequencing Identifies Five Major Classes of Potentially Therapeutic Enzymes Secreted by Lucilia sericata Medical Maggots Zdenjk Franta,1 Heiko Vogel,2 Rüdiger Lehmann,1 Oliver Rupp,3 Alexander Goesmann,3 and Andreas Vilcinskas1,4 1 Department of Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology, Winchesterstraße 2, 35394 Giessen, Germany 2Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knoll-Straße¨ 8, 07745 Jena, Germany 3Justus-Liebig-University of Giessen, Bioinformatics and System Biology, Heinrich-Buff-Ring 58, 35392 Giessen, Germany 4Justus-Liebig-University of Giessen, Institute for Insect Biotechnology, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany Correspondence should be addressed to Andreas Vilcinskas; [email protected] Received 29 January 2016; Accepted 7 March 2016 Academic Editor: Yudong Cai Copyright © 2016 Zdenekˇ Franta et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Lucilia sericata larvae are used as an alternative treatment for recalcitrant and chronic wounds. Their excretions/secretions contain molecules that facilitate tissue debridement, disinfect, or accelerate wound healing and have therefore -
SUMO Protease 1 (GST-Tagged) from Yeast, Recombinant Cat
SUMO Protease 1 (GST-tagged) from Yeast, Recombinant Cat. No. NATE-1708 Lot. No. (See product label) Introduction Description SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the enzyme is active over wide ranges of temperature and pH. After the completion of the cleavage reaction, the protease can be easily removed from the reaction by affinity chromatography using the Glutathione resin. Synonyms Ulp1 peptidase; SUMO Protease; SUMO Protease Product Information Species Yeast Source E. coli Form Liquid EC Number EC 3.4.22.68 Molecular Weight 52.6 kDa (403-621 aa + N-terminal GST). Purity > 90% by SDS-PAGE Activity >10,000 units/mg Concentration 1 mg/ml Unit Definition One unit is defined as the amount of SUMO Protease 1 required to cleave >90% of 5 µg a control protein substrate (SUMO-GFP) in 1 h at 37°C. Creative Enzymes. All rights reserved. 45-1 Ramsey Road, Shirley, NY 11967, USA Tel:1-631-562-8517 1-516-512-3133 Fax:1-631-938-8127 E-mail: [email protected] http://www.creative-enzymes.com Notes INTENDED FOR RESEARCH USE ONLY, NOT FOR USE IN HUMAN, THERAPEUTIC OR DIAGNOSTIC APPLICATIONS. -
United States Patent (19) 11 Patent Number: 5,338,683 Paoletti (45) Date of Patent: "Aug
USOO5338683A United States Patent (19) 11 Patent Number: 5,338,683 Paoletti (45) Date of Patent: "Aug. 16, 1994 54 VACCINIAVIRUS CONTAINING DNA SEQUENCES ENCODING HERPESVIRUS FOREIGN PATENT DOCUMENTS GLY COPROTEINS 0261940 3/1988 European Pat. Off. 9001546 2/1990 PCT Int'l Appl. 75) Inventor: Enzo Paoletti, Albany, N.Y. OTHER PUBLICATIONS 73) Assignee: Health Research Incorporated, Muller et al (1977) J. Gen. Virol. 38, 135-147. Albany, N.Y. Piccini et al (1987) Meth. Enzymol 153, 545-563. Taylor et al (1988) Vaccine 6, 497-507. * Notice: The portion of the term of this patent Perkus et al (1985) Science 229, 981-984. subsequent to Jul. 29, 2003 has been Allen et al. (1987) J. Virol. 61,2454-2461. disclaimed. Piccini et al., Bioessays (Jun. 1986) vol. 5, No. 6, 248-52, at 248. 21 Appl. No.: 502,834 Elliot et al., J. Gen. Virol. (1991), 72, 1762–79, at 1763. Boyle, D. B. et al., J. Gen. Virol. (1986), 67, 1591-1600. 22 Filed: Apr. 4, 1990 Guo et al., J. of Virology, vol. 64, No. 5, pp. 2399-2406 (1990). Related U.S. Application Data Guo et al., J. of Virology, vol. 63, No. 10, pp. 4189-4198 60 Continuation-in-part of Ser. No. 394,488, Aug. 16, (1989). 1989, abandoned, and Ser. No. 90,209, Aug. 27, 1987, Primary Examiner-Elizabeth C. Weimar abandoned, which is a division of Ser. No. 622,135, Assistant Examiner-Deborah Crouch Jun. 9, 1984, Pat. No. 4,722,848, which is a continua Attorney, Agent, or Firm-Curtis, Morris & Safford tion-in-part of Ser. -
Biochemical Investigation of the Ubiquitin Carboxyl-Terminal Hydrolase Family" (2015)
Purdue University Purdue e-Pubs Open Access Dissertations Theses and Dissertations Spring 2015 Biochemical investigation of the ubiquitin carboxyl- terminal hydrolase family Joseph Rashon Chaney Purdue University Follow this and additional works at: https://docs.lib.purdue.edu/open_access_dissertations Part of the Biochemistry Commons, Biophysics Commons, and the Molecular Biology Commons Recommended Citation Chaney, Joseph Rashon, "Biochemical investigation of the ubiquitin carboxyl-terminal hydrolase family" (2015). Open Access Dissertations. 430. https://docs.lib.purdue.edu/open_access_dissertations/430 This document has been made available through Purdue e-Pubs, a service of the Purdue University Libraries. Please contact [email protected] for additional information. *UDGXDWH6FKRRO)RUP 8SGDWHG PURDUE UNIVERSITY GRADUATE SCHOOL Thesis/Dissertation Acceptance 7KLVLVWRFHUWLI\WKDWWKHWKHVLVGLVVHUWDWLRQSUHSDUHG %\ Joseph Rashon Chaney (QWLWOHG BIOCHEMICAL INVESTIGATION OF THE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE FAMILY Doctor of Philosophy )RUWKHGHJUHHRI ,VDSSURYHGE\WKHILQDOH[DPLQLQJFRPPLWWHH Chittaranjan Das Angeline Lyon Christine A. Hrycyna George M. Bodner To the best of my knowledge and as understood by the student in the Thesis/Dissertation Agreement, Publication Delay, and Certification/Disclaimer (Graduate School Form 32), this thesis/dissertation adheres to the provisions of Purdue University’s “Policy on Integrity in Research” and the use of copyrighted material. Chittaranjan Das $SSURYHGE\0DMRU3URIHVVRU V BBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBB BBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBB $SSURYHGE\R. E. Wild 04/24/2015 +HDGRIWKH'HSDUWPHQW*UDGXDWH3URJUDP 'DWH BIOCHEMICAL INVESTIGATION OF THE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE FAMILY Dissertation Submitted to the Faculty of Purdue University by Joseph Rashon Chaney In Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy May 2015 Purdue University West Lafayette, Indiana ii All of this I dedicate wife, Millicent, to my faithful and beautiful children, Josh and Caleb. -
Research Doctorate School in Biomolecular Sciences Doctorate
BIOS Research Doctorate School in BIOmolecular Sciences Doctorate Course in Molecular Biotechnology PhD Thesis Programmed cell death in the megagametophyte of Araucaria bidwillii Hook. post-germinated seeds Student: Dr. SIMONE CASANI Supervisor: Prof. Luciano Galleschi - TABLE OF CONTENTS - ABSTRACT ...............................................................................................................................................5 LIST OF ABBREVIATIONS ...................................................................................................................8 1. INTRODUCTION ................................................................................................................................9 1.1. PROGRAMMED CELL DEATH ....................................................................................... 9 1.2. THE SIGNIFICANCE OF PROGRAMMED CELL DEATH ........................................ 11 1.3. MOLECULAR MECHANISMS OF APOPTOSIS .......................................................... 12 1.4. CASPASES (CYSTEINE ASPARTATE-SPECIFIC PROTEASES) .............................. 17 1.5. MORPHOLOGICAL AND BIOCHEMICAL FEATURES OF APOPTOSIS ............... 20 1.6. PROGRAMMED CELL DEATH IN PLANTS ................................................................ 22 1.6.1. Defence PCD ............................................................................................................... 23 1.6.2. Developmental PCD ................................................................................................... -
Babela Massiliensis, a Representative of A
Pagnier et al. Biology Direct (2015) 10:13 DOI 10.1186/s13062-015-0043-z RESEARCH Open Access Babela massiliensis, a representative of a widespread bacterial phylum with unusual adaptations to parasitism in amoebae Isabelle Pagnier1, Natalya Yutin2, Olivier Croce1, Kira S Makarova2, Yuri I Wolf2, Samia Benamar1, Didier Raoult1, Eugene V Koonin2 and Bernard La Scola1* Abstract Background: Only a small fraction of bacteria and archaea that are identifiable by metagenomics can be grown on standard media. Recent efforts on deep metagenomics sequencing, single-cell genomics and the use of specialized culture conditions (culturomics) increasingly yield novel microbes some of which represent previously uncharacterized phyla and possess unusual biological traits. Results: We report isolation and genome analysis of Babela massiliensis, an obligate intracellular parasite of Acanthamoeba castellanii. B. massiliensis shows an unusual, fission mode of cell multiplication whereby large, polymorphic bodies accumulate in the cytoplasm of infected amoeba and then split into mature bacterial cells. This unique mechanism of cell division is associated with a deep degradation of the cell division machinery and delayed expression of the ftsZ gene. The genome of B. massiliensis consists of a circular chromosome approximately 1.12 megabase in size that encodes, 981 predicted proteins, 38 tRNAs and one typical rRNA operon. Phylogenetic analysis shows that B. massiliensis belongs to the putative bacterial phylum TM6 that so far was represented by the draft genome of the JCVI TM6SC1 bacterium obtained by single cell genomics and numerous environmental sequences. Conclusions: Currently, B. massiliensis is the only cultivated member of the putative TM6 phylum. Phylogenomic analysis shows diverse taxonomic affinities for B.