DOCSLIB.ORG

The Small Gtpases in Fungal Signaling Conservation and Function

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
The Small Gtpases in Fungal Signaling Conservation and Function cells Review The Small GTPases in Fungal Signaling Conservation and Function Mitzuko Dautt-Castro * , Montserrat Rosendo-Vargas and Sergio Casas-Flores * Laboratorio de Genómica Funcional y Comparativa, División de Biología Molecular, IPICYT, San Luis Potosí 78216, Mexico; [email protected] * Correspondence: [email protected] (M.D.-C.); [email protected] (S.C.-F.) Abstract: Monomeric GTPases, which belong to the Ras superfamily, are small proteins involved in many biological processes. They are fine-tuned regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Several families have been identified in organisms from different kingdoms. Overall, the most studied families are Ras, Rho, Rab, Ran, Arf, and Miro. Recently, a new family named Big Ras GTPases was reported. As a general rule, the proteins of all families have five characteristic motifs (G1–G5), and some specific features for each family have been described. Here, we present an exhaustive analysis of these small GTPase families in fungi, using 56 different genomes belonging to different phyla. For this purpose, we used distinct approaches such as phylogenetics and sequences analysis. The main functions described for monomeric GTPases in fungi include morphogenesis, secondary metabolism, vesicle trafficking, and virulence, which are discussed here. Their participation during fungus–plant interactions is reviewed as well. Keywords: small GTPases; Ras; Rho; Rab; Ran; Arf; Miro; BRG; fungi Citation: Dautt-Castro, M.; Rosendo-Vargas, M.; Casas-Flores, S. 1. Overview The Small GTPases in Fungal Small Ras GTPases (rat sarcoma guanine triphosphatases) are monomeric G proteins Signaling Conservation and Function. of low molecular weight (21 to 30 kDa) that are present in all eukaryotes and that participate Cells 2021, 10, 1039. https://doi.org/ in many biological processes. They act as molecular switches, alternating between an active 10.3390/cells10051039 GTP-bound state and an inactive GDP-bound state [1]. This regulation is carried out through the activity of guanine-nucleotide exchange factors (GEFs) and GTPase activating Academic Editor: Bor Luen Tang proteins (GAPs) that catalyze the replacement of GDP by GTP and promote the inactive Received: 15 March 2021 GDP-bound form, respectively (Figure1)[2–4]. Accepted: 23 April 2021 These proteins have a conserved GTP/GDP core and a hydrolysis domain bearing Published: 28 April 2021 five characteristic and highly conserved motifs: G1 (Walker A/P-loop; GxxxxG K[S/T]) implicated in the binding of β- and γ-phosphate groups of the nucleotide; G2 (Switch I; 2+ Publisher’s Note: MDPI stays neutral x[T/S]x) that binds Mg , essential for GTP hydrolysis; G3 (Walker B/Switch II; DxxG) 2 with regard to jurisdictional claims in that interacts with the nucleotide γ-phosphate and Mg ; G4 ([N/T]KxD) that binds directly published maps and institutional affil- to the nucleotide at K and D sites; and G5 (S/CAK/L/T), involved in guanine base iations. recognition [5,6]. The switch I and II regions are flexible segments that sense the nucleotide state and allow the small GTPases to interact with downstream effectors [7,8]. Members of the Small Ras-GTPases superfamily take part in cell regulation, growth, morphogenesis, cell division, and virulence and are known as master regulators of intracel- Copyright: © 2021 by the authors. lular bidirectional vesicle transport [1,9]. They are classified according to their amino acid Licensee MDPI, Basel, Switzerland. sequence and their biochemical properties. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/). Cells 2021, 10, 1039. https://doi.org/10.3390/cells10051039 https://www.mdpi.com/journal/cells Cells 2021, 10, x FOR PEER REVIEW 2 of 29 Cells 2021, 10, 1039 2 of 29 Figure 1. Small GTPases ofof thethe RasRas superfamilysuperfamily regulate regulate several several processes processes in in fungi. fungi. In In fungal fungal cells, cells, GEFs GEFs and and GAPs GAPs catalyze cata- lyzealternation alternation between between an active an active GTP-bound GTP-bound state state and and an inactive an inactive GDP-bound GDP-bound state. state. Active Active GTPase GTPase interacts interacts with with specific spe- cificdownstream downstream effector, effector leading, leading to different to different cell responses. cell responses. The most The representative most representative functions functions of Ras GTPase of Ras familiesGTPase arefamilies listed arein the listed box. in the box. MembersAs shown of in the Figure Small1, Ras the- mostGTPases common superfamily families take and part their in main cell regulation, functions ingrowth, fungi morphogenesare Ras (rat sarcoma),is, cell division, associated and with virulence morphogenesis and are known and virulence as master of fungiregulators with differentof intra- cellularlifestyles, bidirectional such as pathogens, vesicle transport saprobes, [1,9] entomopathogens,. They are classified and mutualists; according Rho to their (Ras amino homo- acidlogue) sequence also known and their as Cdc42/Rho-GTPases, biochemical properties. involved in the regulation of cell polarity, gene expression,As shown and in membrane Figure 1, traffic;the most Rab common (Ras homologue families fromand their brain) main that functions participates in infungi the aresecretion Ras (rat of metabolitessarcoma), associated and lytic enzymeswith morphogenesis [10]; Arf (ADP and ribosylation virulence factors)of fungi participate with differ- in entmembrane/protein lifestyles, such as trafficking pathogens, to thesaprobes, plasma entomopathogens, membrane [9]; Ran and (Ras-like mutualists; nuclear Rho proteins) (Ras homologue)play pivotal rolesalso known in nucleocytoplasmic as Cdc42/Rho- andGTPas nucleares, involved pore transport, in the regulation synthesis of of cell RNA, polar- and ity,as a gene checkpoint expression, of the and cell membrane cycle [11]; traffic; and Miro Rab (mitochondrial (Ras homologue Rho-GTPases), from brain) that also partici- known patesas atypical in the Rhosecretion GTPases, of metabolites serves critical and lytic roles enzymes in mitochondria [10]; Arf (ADP morphology, ribosylation inheritance, factors) participateand homeostasis in membrane/protein [12]. Other less trafficking studied families to the haveplasma been membrane reported, [9] such; Ran as (Ras Era-like-like nuclear(Escherichia proteins) coli Ras-like play pivotal protein), roles involved in nucleocytoplasmic in ribosomal and assembly nuclear [13 pore], and transport, Spg1/Tem1 syn- thesis(Septum of RNA, promoting) and as that a checkpoint participate of in the ring cell constriction, cycle [11]; and septation, Miro (mitochondrial and cell division Rho in- GTPases)Schizosaccharomyces, also known pombe as at[14ypical]. Recently, Rho GTPases, a new fungal serves family critical of roles Ras GTPasesin mitochondria was reported, mor- phology,the Big Ras inheritance GTPases, (BRG), and homeostasis whose main [12] difference. Other isless their studied size, 3- families to 4-times have bigger been com- re- portedpared with, such the as classicalEra-like small(Escherichia GTPases coli as Ras well-like as protein) with their, involved poorly conserved in ribosomal G4 motif. assembly The [13]only, and member Spg1/Tem characterized1 (Septum until promoting) now, TBRG-1 that ofparticipate the plant mutualisticin ring constriction, fungus Trichoderma septation, andvirens cell, is division involved in in Schizosaccharomyces conidiation, development, pombe [14] secondary. Recently, metabolism, a new fungal mycoparasitism, family of Ras GTPasesand biocontrol was reported, [15]. Proteins the Big from Ras the GTPases different (BRG), families whose crosstalk main difference with each otheris their and size, with 3- members of other signal transduction pathways, which together comprise a very large and to 4-times bigger compared with the classical small GTPases as well as with their poorly complex network [9]. conserved G4 motif. The only member characterized until now, TBRG-1 of the plant mu- In this review, we present a comprehensive work where we discuss the state of the tualistic fungus Trichoderma virens, is involved in conidiation, development, secondary art regarding the main families of monomeric GTPases in fungi. Furthermore, we present metabolism, mycoparasitism, and biocontrol [15]. Proteins from the different families analyses at the genomic, phylogenetic, and sequence levels as well as the function of each crosstalk with each other and with members of other signal transduction pathways, which protein family. together comprise a very large and complex network [9]. 2. ClassificationIn this review, and we Phylogenetic present a comprehensive Conservation work of Small where Ras we GTPases discuss inthe Fungi state of the art regarding the main families of monomeric GTPases in fungi. Furthermore, we present Fungi are eukaryotic organisms that are highly relevant ecologically. They differ from analyses at the genomic, phylogenetic, and sequence levels as well as the function of each plants due to their heterotrophic nature, and from animals because they possess cell walls. protein family. Their closest kingdom is the Animalia, from which they diverged nearly 1.3 billion years ago [16,17]. One of their major features is osmotrophy, a way of feeding and nourishment Cells 2021, 10, 1039 3 of 29 that involves the displacement
Load more

Recommended publications
  • Anti-Rab11 Antibody (ARG41900)
    Product datasheet [email protected] ARG41900 Package: 100 μg anti-Rab11 antibody Store at: -20°C Summary Product Description Goat Polyclonal antibody recognizes Rab11 Tested Reactivity Hu, Ms, Rat, Dog, Mk Tested Application IHC-Fr, IHC-P, WB Host Goat Clonality Polyclonal Isotype IgG Target Name Rab11 Antigen Species Mouse Immunogen Purified recombinant peptides within aa. 110 to the C-terminus of Mouse Rab11a, Rab11b and Rab11c (Rab25). Conjugation Un-conjugated Alternate Names RAB11A: Rab-11; Ras-related protein Rab-11A; YL8 RAB11B: GTP-binding protein YPT3; H-YPT3; Ras-related protein Rab-11B RAB25: RAB11C; CATX-8; Ras-related protein Rab-25 Application Instructions Application table Application Dilution IHC-Fr 1:100 - 1:400 IHC-P 1:100 - 1:400 WB 1:250 - 1:2000 Application Note IHC-P: Antigen Retrieval: Heat mediation was recommended. * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control Hepa cell lysate Calculated Mw 24 kDa Observed Size ~ 26 kDa Properties Form Liquid Purification Affinity purification with immunogen. Buffer PBS, 0.05% Sodium azide and 20% Glycerol. Preservative 0.05% Sodium azide www.arigobio.com 1/3 Stabilizer 20% Glycerol Concentration 3 mg/ml Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use.
    [Show full text]
  • Endophytic Fungi: Biological Control and Induced Resistance to Phytopathogens and Abiotic Stresses
    pathogens Review Endophytic Fungi: Biological Control and Induced Resistance to Phytopathogens and Abiotic Stresses Daniele Cristina Fontana 1,† , Samuel de Paula 2,*,† , Abel Galon Torres 2 , Victor Hugo Moura de Souza 2 , Sérgio Florentino Pascholati 2 , Denise Schmidt 3 and Durval Dourado Neto 1 1 Department of Plant Production, Luiz de Queiroz College of Agriculture, University of São Paulo, Piracicaba 13418900, Brazil; [email protected] (D.C.F.); [email protected] (D.D.N.) 2 Plant Pathology Department, Luiz de Queiroz College of Agriculture, University of São Paulo, Piracicaba 13418900, Brazil; [email protected] (A.G.T.); [email protected] (V.H.M.d.S.); [email protected] (S.F.P.) 3 Department of Agronomy and Environmental Science, Frederico Westphalen Campus, Federal University of Santa Maria, Frederico Westphalen 98400000, Brazil; [email protected] * Correspondence: [email protected]; Tel.: +55-54-99646-9453 † These authors contributed equally to this work. Abstract: Plant diseases cause losses of approximately 16% globally. Thus, management measures must be implemented to mitigate losses and guarantee food production. In addition to traditional management measures, induced resistance and biological control have gained ground in agriculture due to their enormous potential. Endophytic fungi internally colonize plant tissues and have the potential to act as control agents, such as biological agents or elicitors in the process of induced resistance and in attenuating abiotic stresses. In this review, we list the mode of action of this group of Citation: Fontana, D.C.; de Paula, S.; microorganisms which can act in controlling plant diseases and describe several examples in which Torres, A.G.; de Souza, V.H.M.; endophytes were able to reduce the damage caused by pathogens and adverse conditions.
    [Show full text]
  • Genome Scale Metabolic Modeling of the Riboflavin Overproducer Ashbya Gossypii
    Chalmers Publication Library Genome Scale Metabolic Modeling of the Riboflavin Overproducer Ashbya gossypii This document has been downloaded from Chalmers Publication Library (CPL). It is the author´s version of a work that was accepted for publication in: Biotechnology and Bioengineering (ISSN: 0006-3592) Citation for the published paper: Ledesma-Amaro, R. ; Kerkhoven, E. ; Revuelta, J. (2014) "Genome Scale Metabolic Modeling of the Riboflavin Overproducer Ashbya gossypii". Biotechnology and Bioengineering, vol. 111(6), pp. 1191-1199. http://dx.doi.org/10.1002/bit.25167 Downloaded from: http://publications.lib.chalmers.se/publication/200098 Notice: Changes introduced as a result of publishing processes such as copy-editing and formatting may not be reflected in this document. For a definitive version of this work, please refer to the published source. Please note that access to the published version might require a subscription. Chalmers Publication Library (CPL) offers the possibility of retrieving research publications produced at Chalmers University of Technology. It covers all types of publications: articles, dissertations, licentiate theses, masters theses, conference papers, reports etc. Since 2006 it is the official tool for Chalmers official publication statistics. To ensure that Chalmers research results are disseminated as widely as possible, an Open Access Policy has been adopted. The CPL service is administrated and maintained by Chalmers Library. (article starts on next page) ARTICLE Genome Scale Metabolic Modeling of the
    [Show full text]
  • Crystal Structure of a Small G Protein in Complex with the Gtpase
    letters to nature of apolipoproteins2,12–14. However, our results show that the residues lipoprotein metabolism involving cell surface heparan sulfate proteoglycans. J. Biol. Chem. 269, 2764– 2+ 2772 (1994). in the conserved acidic motif of LR5 are buried to participate in Ca 16. Innerarity, T. L., Pitas, R. E. & Mahley, R. W. Binding of arginine-rich (E) apoprotein after coordination, instead of being exposed on the surface of the domain recombination with phospholipid vesicles to the low density lipoprotein receptors of fibroblasts. J. Biol. Chem. 254, 4186–4190 (1979). (Fig. 4a). Although lipoprotein uptake by members of the LDLR 17. Otwinowski, Z. & Minor, W. Data Collection and Processing (eds Sawyer, L., Isaacs, N. & Bailey, S.) family may involve an electrostatic component, perhaps through 556–562 (SERC Daresbury Laboratory, Warrington, UK, 1993). association of the lipoproteins with cell-surface proteoglycans15, the 18. CCP4. The SERC (UK) Collaborative Computing Project No. 4 A Suite of Programs for Protein Crystallography (SERC Daresbury Laboratory, Warrington, UK, 1979). LR5 structure demonstrates that the primary role for the conserved 19. Cowtan, K. D. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31, 34–38 (1994). acidic residues in LDL-A modules is structural. It has been noted 20. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 previously that only lipid-associated apolipoproteins bind with (1991). 16 high affinity to the LDLR ; the LR5 structure suggests an alternative 21.
    [Show full text]
  • Protein Prenylation Reactions As Tools for Site-Specific Protein Labeling and Identification of Prenylation Substrates
    Protein prenylation reactions as tools for site-specific protein labeling and identification of prenylation substrates Dissertation zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften (Dr. rer. nat.) des Fachbereichs Chemie der Technischen Universität Dortmund Angefertigt am Max-Planck-Institut für molekulare Physiologie in Dortmund Vorgelegt von Dipl.-Chemikerin Thi Thanh Uyen Nguyen aus Jülich Dortmund, April 2009 Die vorliegende Arbeit wurde in der Zeit von Oktober 2005 bis April 2009 am Max-Planck- Institut für molekulare Physiologie in Dortmund unter der Anleitung von Prof. Dr. Roger S. Goody, Prof. Dr. Kirill Alexandrov und Prof. Dr. Herbert Waldmann durchgeführt. 1. Gutachter : Prof. Dr. R. S. Goody 2. Gutachter : Prof. Dr. H. Waldmann The results of this work were published in the following journals: “Exploiting the substrate tolerance of farnesyltransferase for site-selective protein derivatization” U.T.T. Nguyen, J. Cramer, J. Gomis, R. Reents, M. Gutierrez-Rodriguez, R.S. Goody, K. Alexandrov, H. Waldmann, Chembiochem 2007, 8 (4), 408-23. “Development of selective RabGGTase inhibitors and crystal structure of a RabGGTase- inhibitor complex” Z. Guo, Y.W. Wu, K.T. Tan, R.S. Bon, E. Guiu-Rozas, C. Delon, U.T.T. Nguyen, S. Wetzel,S. Arndt, R.S. Goody, W. Blankenfeldt, K. Alexandrov, H. Waldmann, Angew Chem Int Ed Engl 2008, 47 (20), 3747-50. “Analysis of the eukaryotic prenylome by isoprenoid affinity tagging” U.T.T. Nguyen, Z. Guo, C. Delon, Y.W. Wu, C. Deraeve, B. Franzel, R.S. Bon, W. Blankenfeldt, R.S. Goody, H. Waldmann, D. Wolters, K. Alexandrov, Nat Chem Biol 2009, 5 (4), 227-35.
    [Show full text]
  • Ras Gtpase Chemi ELISA Kit Catalog No
    Ras GTPase Chemi ELISA Kit Catalog No. 52097 (Version B3) Active Motif North America 1914 Palomar Oaks Way, Suite 150 Carlsbad, California 92008, USA Toll free: 877 222 9543 Telephone: 760 431 1263 Fax: 760 431 1351 Active Motif Europe Waterloo Atrium Drève Richelle 167 – boîte 4 BE-1410 Waterloo, Belgium UK Free Phone: 0800 169 31 47 France Free Phone: 0800 90 99 79 Germany Free Phone: 0800 181 99 10 Telephone: +32 (0)2 653 0001 Fax: +32 (0)2 653 0050 Active Motif Japan Azuma Bldg, 7th Floor 2-21 Ageba-Cho, Shinjuku-Ku Tokyo, 162-0824, Japan Telephone: +81 3 5225 3638 Fax: +81 3 5261 8733 Active Motif China 787 Kangqiao Road Building 10, Suite 202, Pudong District Shanghai, 201315, China Telephone: (86)-21-20926090 Hotline: 400-018-8123 Copyright 2021 Active Motif, Inc. www.activemotif.com Information in this manual is subject to change without notice and does not constitute a commit- ment on the part of Active Motif, Inc. It is supplied on an “as is” basis without any warranty of any kind, either explicit or implied. Information may be changed or updated in this manual at any time. This documentation may not be copied, transferred, reproduced, disclosed, or duplicated, in whole or in part, without the prior written consent of Active Motif, Inc. This documentation is proprietary information and protected by the copyright laws of the United States and interna- tional treaties. The manufacturer of this documentation is Active Motif, Inc. © 2021 Active Motif, Inc., 1914 Palomar Oaks Way, Suite 150; Carlsbad, CA 92008.
    [Show full text]
  • Focus on Cdc42 in Breast Cancer: New Insights, Target Therapy Development and Non-Coding Rnas
    Review Focus on Cdc42 in Breast Cancer: New Insights, Target Therapy Development and Non-Coding RNAs Yu Zhang †, Jun Li †, Xing-Ning Lai, Xue-Qiao Jiao, Jun-Ping Xiong and Li-Xia Xiong * Department of Pathophysiology, Jiangxi Province Key Laboratory of Tumor Pathogenesis and Molecular Pathology, Medical College, Nanchang University, 461 Bayi Road, Nanchang 330006, China; [email protected] (Y.Z.); [email protected] (J.L.); [email protected] (X.-N.L.); [email protected] (X.-Q.J.); [email protected] (J.-P.X.) * Correspondence: [email protected]; Tel.: +86-791-8636-0556 † These authors contributed equally to this work. Received: 30 December 2018; Accepted: 8 February 2019; Published: 11 February 2019 Abstract: Breast cancer is the most common malignant tumors in females. Although the conventional treatment has demonstrated a certain effect, some limitations still exist. The Rho guanosine triphosphatase (GTPase) Cdc42 (Cell division control protein 42 homolog) is often upregulated by some cell surface receptors and oncogenes in breast cancer. Cdc42 switches from inactive guanosine diphosphate (GDP)-bound to active GTP-bound though guanine-nucleotide- exchange factors (GEFs), results in activation of signaling cascades that regulate various cellular processes such as cytoskeletal changes, proliferation and polarity establishment. Targeting Cdc42 also provides a strategy for precise breast cancer therapy. In addition, Cdc42 is a potential target for several types of non-coding RNAs including microRNAs and lncRNAs. These non-coding RNAs is extensively involved in Cdc42-induced tumor processes, while many of them are aberrantly expressed. Here, we focus on the role of Cdc42 in cell morphogenesis, proliferation, motility, angiogenesis and survival, introduce the Cdc42-targeted non-coding RNAs, as well as present current development of effective Cdc42-targeted inhibitors in breast cancer.
    [Show full text]
  • Hras Intracellular Trafficking and Signal Transduction Jodi Ho-Jung Mckay Iowa State University
    Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 2007 HRas intracellular trafficking and signal transduction Jodi Ho-Jung McKay Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biological Phenomena, Cell Phenomena, and Immunity Commons, Cancer Biology Commons, Cell Biology Commons, Genetics and Genomics Commons, and the Medical Cell Biology Commons Recommended Citation McKay, Jodi Ho-Jung, "HRas intracellular trafficking and signal transduction" (2007). Retrospective Theses and Dissertations. 13946. https://lib.dr.iastate.edu/rtd/13946 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. HRas intracellular trafficking and signal transduction by Jodi Ho-Jung McKay A dissertation submitted to the graduate faculty in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Major: Genetics Program of Study Committee: Janice E. Buss, Co-major Professor Linda Ambrosio, Co-major Professor Diane Bassham Drena Dobbs Ted Huiatt Iowa State University Ames, Iowa 2007 Copyright © Jodi Ho-Jung McKay, 2007. All rights reserved. UMI Number: 3274881 Copyright 2007 by McKay, Jodi Ho-Jung All rights reserved. UMI Microform 3274881 Copyright 2008 by ProQuest Information and Learning Company. All rights reserved. This microform edition is protected against unauthorized copying under Title 17, United States Code. ProQuest Information and Learning Company 300 North Zeeb Road P.O.
    [Show full text]
  • Colletotrichum – Names in Current Use
    Online advance Fungal Diversity Colletotrichum – names in current use Hyde, K.D.1,7*, Cai, L.2, Cannon, P.F.3, Crouch, J.A.4, Crous, P.W.5, Damm, U. 5, Goodwin, P.H.6, Chen, H.7, Johnston, P.R.8, Jones, E.B.G.9, Liu, Z.Y.10, McKenzie, E.H.C.8, Moriwaki, J.11, Noireung, P.1, Pennycook, S.R.8, Pfenning, L.H.12, Prihastuti, H.1, Sato, T.13, Shivas, R.G.14, Tan, Y.P.14, Taylor, P.W.J.15, Weir, B.S.8, Yang, Y.L.10,16 and Zhang, J.Z.17 1,School of Science, Mae Fah Luang University, Chaing Rai, Thailand 2Research & Development Centre, Novozymes, Beijing 100085, PR China 3CABI, Bakeham Lane, Egham, Surrey TW20 9TY, UK and Royal Botanic Gardens, Kew, Richmond, Surrey TW9 3AB, UK 4Cereal Disease Laboratory, U.S. Department of Agriculture, Agricultural Research Service, 1551 Lindig Street, St. Paul, MN 55108, USA 5CBS-KNAW Fungal Biodiversity Centre, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands 6School of Environmental Sciences, University of Guelph, Guelph, Ontario, N1G 2W1, Canada 7International Fungal Research & Development Centre, The Research Institute of Resource Insects, Chinese Academy of Forestry, Bailongsi, Kunming 650224, PR China 8Landcare Research, Private Bag 92170, Auckland 1142, New Zealand 9BIOTEC Bioresources Technology Unit, National Center for Genetic Engineering and Biotechnology, NSTDA, 113 Thailand Science Park, Paholyothin Road, Khlong 1, Khlong Luang, Pathum Thani, 12120, Thailand 10Guizhou Academy of Agricultural Sciences, Guiyang, Guizhou 550006 PR China 11Hokuriku Research Center, National Agricultural Research Center,
    [Show full text]
  • ADP-Ribosylation Factor, a Small GTP-Binding Protein, Is Required for Binding of the Coatomer Protein Fl-COP to Golgi Membranes JULIE G
    Proc. Natl. Acad. Sci. USA Vol. 89, pp. 6408-6412, July 1992 Biochemistry ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein fl-COP to Golgi membranes JULIE G. DONALDSON*, DAN CASSEL*t, RICHARD A. KAHN*, AND RICHARD D. KLAUSNER* *Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, and tLaboratory of Biological Chemistry, Division of Cancer Treatment, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892 Communicated by Marc Kirschner, April 20, 1992 (receivedfor review February 11, 1992) ABSTRACT The coatomer is a cytosolic protein complex localized to the Golgi complex, although their functions have that reversibly associates with Golgi membranes and is Impli- not been defined. Distinct among these proteins is the ADP- cated in modulating Golgi membrane transport. The associa- ribosylation factor (ARF), originally identified as a cofactor tion of 13-COP, a component of coatomer, with Golgi mem- required for in vitro cholera toxin-catalyzed ADP- branes is enhanced by guanosine 5'-[v-thioltriphosphate ribosylation of the a subunit of the trimeric GTP-binding (GTP[yS]), a nonhydrolyzable analogue of GTP, and by a protein G, (G,.) (19). ARF is an abundant cytosolic protein mixture of aluminum and fluoride ions (Al/F). Here we show that reversibly associates with Golgi membranes (20, 21). that the ADP-ribosylation factor (ARF) is required for the ARF has been shown to be present on Golgi coated vesicles binding of (-COP. Thus, 13-COP contained in a coatomer generated in the presence of GTP[yS], but it is not a com- fraction that has been resolved from ARF does not bind to Golgi ponent of the cytosolic coatomer (22).
    [Show full text]
  • Small Rho Gtpase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis
    University of Denver Digital Commons @ DU Electronic Theses and Dissertations Graduate Studies 1-1-2017 Small Rho GTPase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis Noelle Christine Punessen University of Denver Follow this and additional works at: https://digitalcommons.du.edu/etd Part of the Biology Commons, and the Genetics and Genomics Commons Recommended Citation Punessen, Noelle Christine, "Small Rho GTPase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis" (2017). Electronic Theses and Dissertations. 1337. https://digitalcommons.du.edu/etd/1337 This Thesis is brought to you for free and open access by the Graduate Studies at Digital Commons @ DU. It has been accepted for inclusion in Electronic Theses and Dissertations by an authorized administrator of Digital Commons @ DU. For more information, please contact [email protected],[email protected]. Small Rho GTPase Family Member Cdc42 and its Role in Neuronal Survival and Apoptosis A Thesis Presented to the Faculty of Natural Sciences and Mathematics University of Denver In Partial Fulfillment of the Requirements for the Degree Master of Science by Noelle C. Punessen August 2017 Advisor: Dr. Daniel A. Linseman Author: Noelle C. Punessen Title: Small Rho GTPase Family Member Cdc42 and its Role in Neuronal Survival and Apoptosis Advisor: Dr. Daniel A. Linseman Degree Date: August 2017 Abstract Neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), Alzheimer’s and Parkinson’s disease are caused by a progressive and aberrant destruction of neurons in the brain and spinal cord. These disorders lack effective long term treatments, and existing options focus primarily on either delaying disease onset or alleviating symptomology.
    [Show full text]
  • Clover Anthracnose Caused by Colletotrichum Trifolii
    2 5 2 5 1.0 :; 1111128 1//// . :; 111112 8 11111 . Ww I~ 2.2 : I~ I 2.2 ~ W '"'w Ii£ w ~ ~ ~ ~ ~ 1.1 1.1 ...,a~ ... -- 111111.8 111111.8 '111111. 25 IIIII~ 111111.6 111111.25 111111.4 111111.6 MICROCOPY RESOLUTION TEST CH>XRT (MICROCOPY RESOLUTION TEST CHART NATIONAL BURlAU or SlANO;'RD~·196 H NATiONAL BUREAU OF SlA.NDARDS-1963·A ==========~=~:~========~TECHNICAL BULU'.TIN No. Z8~FEBRUARY. 19Z8 UNITlm:STATES DEPARTMENT OF AGRICULTURE WASHINGTON, D. C. CLOVER ANTHRACNOSE CAUSED BY COLLETOTRICHUM TRIFOLII By JOHN MONTEITH, Jr. ABsociate Pathologist, Office of Vegetable and Forage Diseases, Bureau of Plant Industry 1 CONTENTS Page Page rntroductlon _____________________ 1 The funguR in relntlon to anthrac­ ElIstol'Y and geogro9hlcal dlstrlbu- ., nos~('ontlnul'd. tlon___________________________ 3- Vlabillty Bnd longe't'lty ot DlY~ flost plnnts______________________ lIum and conidia ___________ 13 SYlI1ptom~ _______________________ 3 Dlsspmluution of conidla_______ 13 Inj lIty produced __________________ II Method of Infection and period The cau~,,1 ol'J~nnlsm--------------, 7 of Incubntlon_______________ 13 Tllxonomy __________.:.________ 7 Source of natural Infl'ctlon____ 14 l~olll t1ous____________________ 8 Environmental factors Influencing oc­ Spore germlnntlon ____________ 8 currence and progress of the dla- Cull ural characters ___________ 9 ease__________________________ 15 Helu tlon of tpllIpero ture to '.:'em peruture _________________ 15 growth 011 medIa ___________ \l hlolsture ____________________ 17 Errect of I\ght________________
    [Show full text]