Comparing the Mechanisms of Metal Action in Bacteria: Insight Into Novel Genes Involved in Silver, Gallium and Copper Resistance and Toxicity in Escherichia Coli

Total Page:16

File Type:pdf, Size:1020Kb

Comparing the Mechanisms of Metal Action in Bacteria: Insight Into Novel Genes Involved in Silver, Gallium and Copper Resistance and Toxicity in Escherichia Coli University of Calgary PRISM: University of Calgary's Digital Repository Graduate Studies The Vault: Electronic Theses and Dissertations 2019-07-25 Comparing the mechanisms of metal action in bacteria: insight into novel genes involved in silver, gallium and copper resistance and toxicity in Escherichia coli Gugala, Natalie Gugala, N. (2019). Comparing the mechanisms of metal action in bacteria: insight into novel genes involved in silver, gallium and copper resistance and toxicity in Escherichia coli (Unpublished doctoral thesis). University of Calgary, Calgary, AB. http://hdl.handle.net/1880/110682 doctoral thesis University of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission. Downloaded from PRISM: https://prism.ucalgary.ca Gene Names GO terms (biological process) Score aaeA aaeA // "yhcQ"carboxylic // "b3241" acid // transport "ECK3230" // "transmembrane transport" -0.0487841 aaeB aaeB // "yhcP"transmembrane // "b3240" // "ECK3229"transport // "carboxylic acid transport" 0.10667059 aaeR aaeR // "yhcS"positive // "qseA" regulation // "b3243" of transcription, // "ECK3232" DNA-templated // "DNA-templated0.18076241 transcription, initiation" // "regulation of transcription, DNA-templated" // "transcription, DNA-templated" aaeX aaeX // "yhcR" // "b3242" // "ECK3231" 0.06718923 aas aas // "b2836"phospholipid // "ECK2832" biosynthetic process // "metabolic process" // "fatty0.30458777 acid metabolic process" aat aat // "ycaA"protein // "b0885" catabolic // "ECK0876" process -0.0732 abgA abgA // "ydaJ"proteolysis // "b1338" // //"folic "ECK1334" acid catabolic process" 0.08978529 abgB abgB // "ydaI"proteolysis // "b1337" // // "folic "ECK1333" acid catabolic process" 0.22717458 abgR abgR // "b1339"regulation // "ECK1335" of transcription, DNA-templated // "transcription, DNA-templated"0.06734757 abgT abgT // "ydaH"p-aminobenzoyl-glutamate // "b1336" // "ECK1332" transmembrane transport // "amino-0.1126479 acid transport" // "p-aminobenzoyl-glutamate transport" abrB abrB // "ybgN"regulation // "b0715" of gene// "ECK0704" expression -0.0573451 aceA aceA // "icl" //carboxylic "b4015" acid // "ECK4007" metabolic process // "tricarboxylic acid cycle" // "glyoxylate0.2981715 cycle" aceB aceB // "mas"tricarboxylic // "b4014" acid // "ECK4006" cycle // "glyoxylate cycle" -0.0520439 aceE aceE // "b0114"oxidation-reduction // "ECK0113" process // "glycolytic process" 0.08209107 aceF aceF // "b0115"pyruvate // "ECK0114" metabolic process // "acetyl-CoA biosynthetic process -0.0435432from pyruvate" // "glycolytic process" aceK aceK // "b4016"peptidyl-serine // "ECK4008" dephosphorylation // "phosphorylation" // "glucose-0.018376 metabolic process" // "peptidyl-serine phosphorylation" // "regulation of catalytic activity" // "tricarboxylic acid cycle" // "glyoxylate cycle" ackA ackA // "b2296"single-species // "ECK2290" biofilm formation on inanimate substrate // "acetate0.11404148 metabolic process" // "organic acid metabolic process" // "propionate biosynthetic process" // "acetate biosynthetic process" // "acetyl-CoA biosynthetic process" // "phosphorylation" acnA acnA // "acn"citrate // "b1276" metabolic // "ECK1271" process // "glyoxylate cycle" // "anaerobic respiration"-0.2655182 // "response to oxidative stress" // "tricarboxylic acid cycle" acnB acnB // "yacJ"regulation // "yacI" of// translation"b0118" // //"ECK0117" "glyoxylate cycle" // "propionate catabolic0.03648468 process, 2-methylcitrate cycle" // "tricarboxylic acid cycle" acpT acpT // "yhhU"lysine // "b3475" biosynthetic // "ECK3459" process via aminoadipic acid // "peptidyl-serine0.03735872 phosphopantetheinylation" // "fatty acid biosynthetic process" acrA acrA // "sipB"drug // "Mb" transmembrane // "lir" // "mbl" transport // "mtcA" // "response // "nbsA" to //toxic "b0463" substance" // "ECK0457"-0.0131383 // "alkane transport" // "fatty acid transport" // "response to drug" // "drug transmembrane export" // "bile acid and bile salt transport" // "transmembrane transport" // "response to antibiotic" acrB acrB // "acrE"transmembrane // "b0462" // "ECK0456" transport // "drug transmembrane transport" 0.27424717// "response to antibiotic" // "alkane transport" // "fatty acid transport" // "enterobactin transport" // "response to toxic substance" // "bile acid and bile salt transport" // "drug transmembrane export" // "drug export" // "response to drug" acrD acrD // "yffA"response // "b2470" to antibiotic// "ECK2465" // "response to toxic substance" // "bile acid-0.0236443 and bile salt transport" // "drug transmembrane export" // "transmembrane transport" // "drug export" // "drug transmembrane transport" acrE acrE // "envC"response // "b3265" to drug // "ECK3252" // "drug transmembrane transport" // "response0.0937572 to antibiotic" // "transmembrane transport" acrF acrF // "envD"transmembrane // "b3266" // "ECK3253" transport // "drug transmembrane transport" -0.2791022 acrR acrR // "ybaH"negative // "b0464" regulation // "ECK0458" of transcription, DNA-templated // "response0.16977651 to drug" // "transcription, DNA-templated" acs acs // "yfaC" chemotaxis// "acsA" // // "b4069" "protein // deacetylation" "ECK4062" // "post-translational protein-0.0652781 acetylation" // "peptidyl-lysine acetylation" // "acetyl-CoA biosynthetic process from acetate" // "acetate catabolic process" actP actP // "yjcG"tellurite // "b4067" transport // "ECK4060" // "glycolate transmembrane transport" // "transmembrane-0.1122096 transport" // "ion transport" // "plasma membrane acetate transport" // "sodium ion transport" ada ada // "b2213"peptidyl-cysteine // "ECK2205" methylation // "positive regulation of transcription,0.25814502 DNA-templated" // "negative regulation of transcription, DNA-templated" // "metabolic process" // "DNA demethylation" // "regulation of transcription, DNA-templated" // "DNA dealkylation involved in DNA repair" // "methylation" // "cellular response to DNA damage stimulus" // "DNA repair" add add // "b1623"inosine // "ECK1618" biosynthetic process // "hypoxanthine biosynthetic process"-0.3914476 // "hypoxanthine salvage" // "purine nucleotide salvage" // "purine nucleotide interconversion" // "adenosine catabolic process" // "purine ribonucleoside monophosphate biosynthetic process" // "nucleotide metabolic process" // "cellular response to DNA damage stimulus" ade -0.0436342 adhE adhE // "adhC"metabolic // "ana" process // "b1241" // "alcohol // "ECK1235" metabolic process" // "carbon utilization"0.09847238 // "ethanol biosynthetic process" // "oxidation-reduction process" adhP adhP // "yddN"acetaldehyde // "b1478" catabolic// "ECK1472" process // "response to ethanol" // "cellular0.1536338 response to DNA damage stimulus" // "oxidation-reduction process" adiA adiA // "adi" cellular// "b4117" amino // "ECK4110"acid metabolic process // "arginine catabolic process"0.01161927 // "intracellular pH elevation" adiC adiC // "yjdD"transmembrane // "yjdE" // "b4115" transport // "ECK4108" // "arginine transmembrane transport"-0.0074044 // "amino acid transport" // "amino acid transmembrane transport" // "intracellular pH elevation" adiY adiY // "b4116"regulation // "ECK4109" of transcription, DNA-templated // "positive regulation0.12767056 of transcription, DNA-templated" aegA aegA // "yffG"glutamate // "b2468" biosynthetic // "ECK2463" process // "oxidation-reduction process"-0.0233589 aer aer // "yqjJ" //chemotaxis "air" // "b3072" // "positive // "ECK3062" aerotaxis" // "signal transduction" 0.08846473 aes aes // "ybaC"negative // "b0476" regulation // "ECK0470" of DNA-binding transcription factor activity 0.05525018// "negative regulation of hydrolase activity" afuB afuB // "fbpB" // "b0263" // "ECK0265" 0.02257587 afuC afuC // "fbpC"iron // "yagC"import //into "b0262" cell // "iron// "ECK0264" ion transport" // "ATP hydrolysis coupled-0.0307568 cation transmembrane transport" // "transmembrane transport" // "iron ion homeostasis" // "ion transport" agaA agaA // "yraA" // "b3135" // "ECK3123" -0.0206907 agaB agaB // "yraD"carbohydrate // "b3138" transmembrane// "ECK3126" transport // "phosphorylation" //0.00297853 "carbohydrate transport" // "phosphoenolpyruvate-dependent sugar phosphotransferase system" agaC agaC // "yraE"carbohydrate // "b3139" //transport "ECK3127" // "phosphoenolpyruvate-dependent sugar0.12460596 phosphotransferase system" agaD agaD // "yraF"phosphoenolpyruvate-dependent // "b3140" // "ECK3128" sugar phosphotransferase system0.19496 // "carbohydrate transport" agaI agaI // "yraG"N-acetylneuraminate // "b3141" // "ECK3129" catabolic process // "UDP-N-acetylglucosamine-0.0087468 biosynthetic process" // "N-acetylglucosamine catabolic process" // "glucosamine catabolic process" // "N-acetylglucosamine metabolic process" // "carbohydrate metabolic process" agaR agaR // "yhaW"regulation // "b3131" of transcription, // "ECK3119" DNA-templated -0.3003171 agaS agaS // "yraB"carbohydrate // "b3136" //derivative "ECK3124" metabolic process // "phosphoenolpyruvate-dependent0.28130805 sugar phosphotransferase system" agaV agaV // "yhaY"carbohydrate // "b3133" transmembrane// "ECK3121" transport // "phosphorylation" //0.14020971 "phosphoenolpyruvate-dependent sugar phosphotransferase system" // "carbohydrate transport" agaW agaW // "yhaZ" // "b3134" // "ECK3122" -0.0899568
Recommended publications
  • SCHELVIS CV Profile 2010
    Curriculum vitae: Johannes Schelvis 09/7/2010 PERSONAL INFORMATION Johannes P. M. Schelvis, Associate Professor Montclair State University Department of Chemistry and Biochemistry 1 Normal Avenue Montclair, NJ 07043 EDUCATION B.S., Physics, 1985, Free University, Amsterdam, Netherlands Ph.D., Biophysics, 1995, University of Leiden, Leiden, Netherlands PROFESSIONAL EXPERIENCE Associate Professor Montclair State University September 2007 – present Assistant Professor New York University September 2000 – August 2007 Postdoctoral Researcher Michigan State University March 1995 - August 2000 HONORS AND AWARDS • Institute Fellow, Margaret and Herman Sokol Institute for the Pharmaceutical Life Sciences at Montclair State University, September 2008 - present • Goddard Fellowship, New York University, 2004 • Whitehead Fellowship for Junior Faculty in Biomedical or Biological Sciences, New York University, 2003. GRANTS AWARDED ACTIVE • "Molecular Mechanisms of Photolyase and Cryptochrome" National Science Foundation, MCB-0920013, August 2009 – July 2012 , $419,453 t.c. (PI) • "Binding of ICER to Its Own Promoter as a Mode of Cooperative Regulation" Margaret and Herman Sokol Institute for Pharmaceutical Life Sciences, September 2008 – August 2011 (1-year no cost extension), $100,000 (PI with Dr. Carlos Molina) • "Light-Driven Damage and Repair of DNA", Faculty Scholarship Program, Montclair State University, 2008 – 2012 , 6 TCH (PI) COMPLETED • "Fingerprinting DNA Damage" Margaret and Herman Sokol Faculty/Student Research Grant Program, July 2008
    [Show full text]
  • Characterisation, Classification and Conformational Variability Of
    Characterisation, Classification and Conformational Variability of Organic Enzyme Cofactors Julia D. Fischer European Bioinformatics Institute Clare Hall College University of Cambridge A thesis submitted for the degree of Doctor of Philosophy 11 April 2011 This dissertation is the result of my own work and includes nothing which is the outcome of work done in collaboration except where specifically indicated in the text. This dissertation does not exceed the word limit of 60,000 words. Acknowledgements I would like to thank all the members of the Thornton research group for their constant interest in my work, their continuous willingness to answer my academic questions, and for their company during my time at the EBI. This includes Saumya Kumar, Sergio Martinez Cuesta, Matthias Ziehm, Dr. Daniela Wieser, Dr. Xun Li, Dr. Irene Pa- patheodorou, Dr. Pedro Ballester, Dr. Abdullah Kahraman, Dr. Rafael Najmanovich, Dr. Tjaart de Beer, Dr. Syed Asad Rahman, Dr. Nicholas Furnham, Dr. Roman Laskowski and Dr. Gemma Holli- day. Special thanks to Asad for allowing me to use early development versions of his SMSD software and for help and advice with the KEGG API installation, to Roman for knowing where to find all kinds of data, to Dani for help with R scripts, to Nick for letting me use his E.C. tree program, to Tjaart for python advice and especially to Gemma for her constant advice and feedback on my work in all aspects, in particular the chemistry side. Most importantly, I would like to thank Prof. Janet Thornton for giving me the chance to work on this project, for all the time she spent in meetings with me and reading my work, for sharing her seemingly limitless knowledge and enthusiasm about the fascinating world of enzymes, and for being such an experienced and motivational advisor.
    [Show full text]
  • Cheminformatics for Genome-Scale Metabolic Reconstructions
    CHEMINFORMATICS FOR GENOME-SCALE METABOLIC RECONSTRUCTIONS John W. May European Molecular Biology Laboratory European Bioinformatics Institute University of Cambridge Homerton College A thesis submitted for the degree of Doctor of Philosophy June 2014 Declaration This thesis is the result of my own work and includes nothing which is the outcome of work done in collaboration except where specifically indicated in the text. This dissertation is not substantially the same as any I have submitted for a degree, diploma or other qualification at any other university, and no part has already been, or is currently being submitted for any degree, diploma or other qualification. This dissertation does not exceed the specified length limit of 60,000 words as defined by the Biology Degree Committee. This dissertation has been typeset using LATEX in 11 pt Palatino, one and half spaced, according to the specifications defined by the Board of Graduate Studies and the Biology Degree Committee. June 2014 John W. May to Róisín Acknowledgements This work was carried out in the Cheminformatics and Metabolism Group at the European Bioinformatics Institute (EMBL-EBI). The project was fund- ed by Unilever, the Biotechnology and Biological Sciences Research Coun- cil [BB/I532153/1], and the European Molecular Biology Laboratory. I would like to thank my supervisor, Christoph Steinbeck for his guidance and providing intellectual freedom. I am also thankful to each member of my thesis advisory committee: Gordon James, Julio Saez-Rodriguez, Kiran Patil, and Gos Micklem who gave their time, advice, and guidance. I am thankful to all members of the Cheminformatics and Metabolism Group.
    [Show full text]
  • Significance of Heme and Heme Degradation in the Pathogenesis Of
    International Journal of Molecular Sciences Review Significance of Heme and Heme Degradation in the Pathogenesis of Acute Lung and Inflammatory Disorders Stefan W. Ryter Proterris, Inc., Boston, MA 02118, USA; [email protected] Abstract: The heme molecule serves as an essential prosthetic group for oxygen transport and storage proteins, as well for cellular metabolic enzyme activities, including those involved in mitochondrial respiration, xenobiotic metabolism, and antioxidant responses. Dysfunction in both heme synthesis and degradation pathways can promote human disease. Heme is a pro-oxidant via iron catalysis that can induce cytotoxicity and injury to the vascular endothelium. Additionally, heme can modulate inflammatory and immune system functions. Thus, the synthesis, utilization and turnover of heme are by necessity tightly regulated. The microsomal heme oxygenase (HO) system degrades heme to carbon monoxide (CO), iron, and biliverdin-IXα, that latter which is converted to bilirubin-IXα by biliverdin reductase. Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms. Therapeutic strategies targeting the heme/HO-1 pathway, including therapeutic modulation of heme levels, elevation (or inhibition) of HO-1 protein and activity, and application of CO donor compounds or gas show potential in inflammatory conditions including sepsis and pulmonary diseases. Keywords: acute lung injury; carbon monoxide; heme; heme oxygenase; inflammation; lung dis- ease; sepsis Citation: Ryter, S.W. Significance of Heme and Heme Degradation in the Pathogenesis of Acute Lung and Inflammatory Disorders. Int. J. Mol. 1. Introduction Sci.
    [Show full text]
  • Evolution of the Heme Biosynthetic Pathway in Eukaryotic Phototrophs
    School of Doctoral Studies in Biological Sciences University of South Bohemia in České Budějovice Faculty of Science Evolution of the Heme Biosynthetic Pathway in Eukaryotic Phototrophs Ph.D. Thesis Mgr. Jaromír Cihlář Supervisor: Prof. Ing. Miroslav Oborník, Ph.D. Biology Centre CAS v.v.i., Institute of Parasitology České Budějovice 2018 This thesis should be cited as: Cihlář J., 2018. Evolution of the Heme Biosynthetic Pathway in Eukaryotic Phototrophs. Ph.D. Thesis Series, University of South Bohemia, Faculty of Science, School of Doctoral Studies in Biological Sciences, České Budějovice, Czech Republic. Annotation This thesis is devoted to the evolution of the heme biosynthetic pathway in eukaryotic phototrophs with particular emphasis on algae possessing secondary and tertiary red and green derived plastids. Based on molecular biology and bioinformatics approaches it explores the diversity and similarities in heme biosynthesis among different algae. The core study of this thesis describes the heme biosynthesis in Bigelowiella natans and Guillardia theta, algae containing a remnant endosymbiont nucleus within their plastids, in dinoflagellates containing tertiary endosymbionts derived from diatoms – called dinotoms, and in Lepidodinium chlorophorum, a dinoflagellate containing a secondary green plastid. The thesis further focusses on new insights in the heme biosynthetic pathway and general origin of the genes in chromerids the group of free-living algae closely related to apicomplexan parasites. Declaration [in Czech] Prohlašuji, že svoji disertační práci jsem vypracoval samostatně pouze s použitím pramenů a literatury uvedených v seznamu citované literatury. Prohlašuji, že v souladu s § 47b zákona č. 111/1998 Sb. v platném znění souhlasím se zveřejněním své disertační práce, a to v nezkrácené podobě elektronickou cestou ve veřejně přístupné části databáze STAG provozované Jihočeskou univerzitou v Českých Budějovicích na jejích internetových stránkách, a to se zachováním mého autorského práva k odevzdanému textu této kvalifikační práce.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2016/0186168 A1 Konieczka Et Al
    US 2016O1861 68A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2016/0186168 A1 Konieczka et al. (43) Pub. Date: Jun. 30, 2016 (54) PROCESSES AND HOST CELLS FOR Related U.S. Application Data GENOME, PATHWAY. AND BIOMOLECULAR (60) Provisional application No. 61/938,933, filed on Feb. ENGINEERING 12, 2014, provisional application No. 61/935,265, - - - filed on Feb. 3, 2014, provisional application No. (71) Applicant: ENEVOLV, INC., Cambridge, MA (US) 61/883,131, filed on Sep. 26, 2013, provisional appli (72) Inventors: Jay H. Konieczka, Cambridge, MA cation No. 61/861,805, filed on Aug. 2, 2013. (US); James E. Spoonamore, Publication Classification Cambridge, MA (US); Ilan N. Wapinski, Cambridge, MA (US); (51) Int. Cl. Farren J. Isaacs, Cambridge, MA (US); CI2N 5/10 (2006.01) Gregory B. Foley, Cambridge, MA (US) CI2N 15/70 (2006.01) CI2N 5/8 (2006.01) (21) Appl. No.: 14/909, 184 (52) U.S. Cl. 1-1. CPC ............ CI2N 15/1082 (2013.01); C12N 15/81 (22) PCT Filed: Aug. 4, 2014 (2013.01); C12N 15/70 (2013.01) (86). PCT No.: PCT/US1.4/49649 (57) ABSTRACT S371 (c)(1), The present disclosure provides compositions and methods (2) Date: Feb. 1, 2016 for genomic engineering. Patent Application Publication Jun. 30, 2016 Sheet 1 of 4 US 2016/O186168 A1 Patent Application Publication Jun. 30, 2016 Sheet 2 of 4 US 2016/O186168 A1 &&&&3&&3&&**??*,º**)..,.: ××××××××××××××××××××-************************** Patent Application Publication Jun. 30, 2016 Sheet 3 of 4 US 2016/O186168 A1 No.vaegwzºkgwaewaeg Patent Application Publication Jun. 30, 2016 Sheet 4 of 4 US 2016/O186168 A1 US 2016/01 86168 A1 Jun.
    [Show full text]
  • Supplementary Data
    Supplemental Material Materials and Methods Immunohistochemistry Primary antibodies used for validation studies include: mouse anti-desmoglein-3 (Cat. # 32-6300, Invitrogen, CA, USA; 1:25), rabbit anti-cytokeratin 4 (Cat. # ab11215, Abcam, Cambridge, MA, USA; 1:100), mouse anti-cytokeratin 16 (Cat. # ab8741, Abcam; 1:25), rabbit anti-desmoplakin antibody (Cat. # ab14418, Abcam; 1:200), mouse anti-vimentin (Cat. # M7020, Dako, Carpinteria, CA, USA; 1:100). Secondary antibodies conjugated with biotin (Vector, Burlingame, CA, USA) were used, diluted to 1:400. Tissues slides containing archival FFPE sections, or tissue micro arrays (TMA) consisting of 508 HNSCC and controls, were dewaxed in SafeClear II (Fisher Scientific, Pittsburgh, PA, USA) hydrated through graded alcohols, immersed in 3% hydrogen peroxide in PBS for 30 min to quench the endogenous peroxidase, and processed for antigen retrieval and immunostaining with the appropriate primary antibodies and biotinylated secondary antibodies as described (1), followed by the avidin-biotin complex method (Vector Stain Elite, ABC kit; Vector). Slides were washed and developed in 3,3'- diaminobenzidine (Sigma FASTDAB tablet; Sigma Chemical) under microscopic control, and counterstained with Mayer's hematoxylin. For each stained TMA the number of positive cells in each core was visually evaluated and the results expressed as a percentage of stained cells/ total number of cells. According to their immunoreactivity the tissues array cores were divided according to tumor differentiation, where the percentage of stained cells in the three tumor classes were scored as more than 5% and less than 25% of the cells stained, 26 to 50%, 51 to 75% or, 75 to 100%.
    [Show full text]
  • Supplemental Table S1: Comparison of the Deleted Genes in the Genome-Reduced Strains
    Supplemental Table S1: Comparison of the deleted genes in the genome-reduced strains Legend 1 Locus tag according to the reference genome sequence of B. subtilis 168 (NC_000964) Genes highlighted in blue have been deleted from the respective strains Genes highlighted in green have been inserted into the indicated strain, they are present in all following strains Regions highlighted in red could not be deleted as a unit Regions highlighted in orange were not deleted in the genome-reduced strains since their deletion resulted in severe growth defects Gene BSU_number 1 Function ∆6 IIG-Bs27-47-24 PG10 PS38 dnaA BSU00010 replication initiation protein dnaN BSU00020 DNA polymerase III (beta subunit), beta clamp yaaA BSU00030 unknown recF BSU00040 repair, recombination remB BSU00050 involved in the activation of biofilm matrix biosynthetic operons gyrB BSU00060 DNA-Gyrase (subunit B) gyrA BSU00070 DNA-Gyrase (subunit A) rrnO-16S- trnO-Ala- trnO-Ile- rrnO-23S- rrnO-5S yaaC BSU00080 unknown guaB BSU00090 IMP dehydrogenase dacA BSU00100 penicillin-binding protein 5*, D-alanyl-D-alanine carboxypeptidase pdxS BSU00110 pyridoxal-5'-phosphate synthase (synthase domain) pdxT BSU00120 pyridoxal-5'-phosphate synthase (glutaminase domain) serS BSU00130 seryl-tRNA-synthetase trnSL-Ser1 dck BSU00140 deoxyadenosin/deoxycytidine kinase dgk BSU00150 deoxyguanosine kinase yaaH BSU00160 general stress protein, survival of ethanol stress, SafA-dependent spore coat yaaI BSU00170 general stress protein, similar to isochorismatase yaaJ BSU00180 tRNA specific adenosine
    [Show full text]
  • Genome-Scale Metabolic Network Analysis and Drug Targeting of Multi-Drug Resistant Pathogen Acinetobacter Baumannii AYE
    Electronic Supplementary Material (ESI) for Molecular BioSystems. This journal is © The Royal Society of Chemistry 2017 Electronic Supplementary Information (ESI) for Molecular BioSystems Genome-scale metabolic network analysis and drug targeting of multi-drug resistant pathogen Acinetobacter baumannii AYE Hyun Uk Kim, Tae Yong Kim and Sang Yup Lee* E-mail: [email protected] Supplementary Table 1. Metabolic reactions of AbyMBEL891 with information on their genes and enzymes. Supplementary Table 2. Metabolites participating in reactions of AbyMBEL891. Supplementary Table 3. Biomass composition of Acinetobacter baumannii. Supplementary Table 4. List of 246 essential reactions predicted under minimal medium with succinate as a sole carbon source. Supplementary Table 5. List of 681 reactions considered for comparison of their essentiality in AbyMBEL891 with those from Acinetobacter baylyi ADP1. Supplementary Table 6. List of 162 essential reactions predicted under arbitrary complex medium. Supplementary Table 7. List of 211 essential metabolites predicted under arbitrary complex medium. AbyMBEL891.sbml Genome-scale metabolic model of Acinetobacter baumannii AYE, AbyMBEL891, is available as a separate file in the format of Systems Biology Markup Language (SBML) version 2. Supplementary Table 1. Metabolic reactions of AbyMBEL891 with information on their genes and enzymes. Highlighed (yellow) reactions indicate that they are not assigned with genes. No. Metabolism EC Number ORF Reaction Enzyme R001 Glycolysis/ Gluconeogenesis 5.1.3.3 ABAYE2829
    [Show full text]
  • Timothy P. Driscolla, Victoria I. Verhoevea, Mark L. Guillotteb
    Wholly Rickettsia! Metabolic Profile of the Quintessential Bacterial Parasite of Eukaryotic Cells Item Type Poster/Presentation Authors Driscoll, Timothy P.; Verhoeve, Victoria I.; Guillotte, Mark L.; Lehman, Stephanie S.; Rennoll, Sherri A.; Beier-Sexton, Magda; Rahman, M. Sayeedur; Azad, Abdu F.; Gillespie, Joseph J. Publication Date 2018-06 Keywords Metabolic Networks and Pathways; Rickettsia--genetics; Rickettsia--metabolism Download date 01/10/2021 05:45:11 Link to Item http://hdl.handle.net/10713/16003 Wholly Rickettsia! Metabolic Profile of the Quintessential Bacterial Parasite of Eukaryotic Cells Timothy Driscoll a a b b b b b b b Timothy P. Driscoll , Victoria I. Verhoeve , Mark L. Guillotte , Stephanie S. Lehman , Sherri A. Rennoll , Magda Beier-Sexton , M. Sayeedur Rahman , Abdu F. Azad , and Joseph J. Gillespie [email protected] Department of Biology, West Virginia University, Morgantown, WV 26505, USAa; Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201, USAb @driscollMML (twitter, fb, reddit, github) BACKGROUND RESULTS Figure 2. Synopsis of known and predicted metabolites imported from Figure 3. Fatty acids and glycerophospholipids are synthesized Figure 5A. Cell envelope glycoconjugates are synthesized from Bacteria in the genus Rickettsia (Rickettsiaceae; Alphaproteobacteria) Our metabolic reconstruction (Fig. 1) identified 51 host metabolites (including 21 the eukaryotic cytoplasm by rickettsiae. from host precursors dephospho-CoA and biotin, DHAP and
    [Show full text]
  • Decoding Cytochrome C Oxidase Biogenesis: New Insights Into Copper Trafficking
    University of Pennsylvania ScholarlyCommons Publicly Accessible Penn Dissertations 2011 Decoding Cytochrome C Oxidase Biogenesis: New Insights Into Copper Trafficking Nursel Seda Ekici University of Pennsylvania, [email protected] Follow this and additional works at: https://repository.upenn.edu/edissertations Part of the Biology Commons, Genetics Commons, and the Molecular Biology Commons Recommended Citation Ekici, Nursel Seda, "Decoding Cytochrome C Oxidase Biogenesis: New Insights Into Copper Trafficking" (2011). Publicly Accessible Penn Dissertations. 474. https://repository.upenn.edu/edissertations/474 This paper is posted at ScholarlyCommons. https://repository.upenn.edu/edissertations/474 For more information, please contact [email protected]. Decoding Cytochrome C Oxidase Biogenesis: New Insights Into Copper Trafficking Abstract Acquisition, delivery and incorporation of metals to their respective metalloproteins are important cellular processes. These processes are tightly controlled so that cells are not exposed to free metal concentrations that would lead to harmful oxidative damages. Cytochrome c oxidases (Cox) are among these metalloproteins whose assembly and activity involves incorporation of Cu cofactor into their catalytic subunits in addition to the maturation of other subunits. In this study, we focused on the pathways of acquisition of Cu by the facultative phototroph Rhodobacter capsulatus for incorporation into the heme–Cu binuclear center of its cbb3–type Cox (cbb3–Cox). Genetic screens identified a 2+ cbb3–Cox defective mutant that requires Cu supplement to produce an active cbb3–Cox. Complementation of this mutant using wild-type genomic libraries unveiled a novel gene (ccoA) required for cbb3–Cox biogenesis in R. capsulatus. In the absence of CcoA, cellular content of Cu decreases, and cbb3–Cox assembly and activity becomes defective.
    [Show full text]
  • Occurrence of Heme O in Photoheterotrophically Growing, Semi-Anaerobic Cyanobacterium Synechocystis Sp. PCC6803 Giinter A
    FEBS 15893 FEBS Letters 371 (1995) 89-93 Occurrence of heme O in photoheterotrophically growing, semi-anaerobic cyanobacterium Synechocystis sp. PCC6803 Giinter A. Peschek*, Marnik Wastyn, Susanne Fromwald, Bernhard Mayer Biophysical Chemistry Group, Institute of Physical Chemistry, University of Vienna, Wiihringerstrasse 42, A-1090 Vienna, Austria Received 12 June 1995; revised version received 10 July 1995 a period of simple detoxification, it must have proven of much Abstract Extraction and identification of the non-covalently greater evolutionary and ecological significance to transform bound heme groups from crude membrane preparations of pho- the pre-existing biochemical systems of photosynthesis (most toheterotrophically grown Synechocystis sp. PCC 6803 by re- importantly: the membrane-bound electron transport assem- versed phase high performance liquid chromatography and opti- bly) into aerobic respiration and a respiratory chain ('conver- cal spectrophotometry led to the detection of heme O in addition sion hypothesis'; see [3,9,10]) and thus to eliminate the 02 by to heroes B and A which latter was to be expected from the known reducing it back to water. presence of aa3-type cytochrome oxidase in cyanobacteria. In fully aerated cells (245 pM dissolved O2 in the medium) besides In this context it is worth noting that all of the cyanobacteria heme B only heine A was found while in low-oxygen cells (< 10 investigated so far (twenty-seven different strains and species pM dissolved 02) heme O was present at a concentration even tested) synthesize an aa3-type cytochrome-c oxidase ([11]; Pe- higher than that of heme A. Given the possible role of heme O schek et al., unpublished).
    [Show full text]