ISPP 2012 14Th Internacional Symposium on Phototrophic Prokaryotes Abstract Book
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Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents
International Journal of Molecular Sciences Article Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents 1, 2,3, 1 2, Elena V. Eremeeva y , Tianyu Jiang y , Natalia P. Malikova , Minyong Li * and Eugene S. Vysotski 1,* 1 Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk 660036, Russia; [email protected] (E.V.E.); [email protected] (N.P.M.) 2 Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan 250012, China; [email protected] 3 State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao 266237, China * Correspondence: [email protected] (M.L.); [email protected] (E.S.V.); Tel.: +86-531-8838-2076 (M.L.); +7-(391)-249-44-30 (E.S.V.); Fax: +86-531-8838-2076 (M.L.); +7-(391)-290-54-90 (E.S.V.) These authors contributed equally to this work. y Received: 23 June 2020; Accepted: 27 July 2020; Published: 30 July 2020 Abstract: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. -
Discovery and Protein Engineering of Baeyer-Villiger Monooxygenases
Discovery and Protein Engineering of Baeyer-Villiger monooxygenases Inauguraldissertation zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften (Dr. rer. nat.) der Mathematisch-Naturwissenschaftlichen Fakultät der Ernst-Moritz-Arndt-Universität Greifswald vorgelegt von Andy Beier geboren am 11.10.1988 in Parchim Greifswald, den 02.08.2017 I Dekan: Prof. Dr. Werner Weitschies 1. Gutachter: Prof. Dr. Uwe T. Bornscheuer 2. Gutachter: Prof. Dr. Marko Mihovilovic Tag der Promotion: 24.10.2017 II We need to learn to want what we have, not to have what we want, in order to get stable and steady happiness. - The Dalai Lama - III List of abbreviations % Percent MPS Methyl phenyl sulfide % (v/v) % volume per volume MPSO Methyl phenyl sulfoxide % (w/v) % weight per volume MPSO2 Methyl phenyl sulfone °C Degrees Celsius MTS Methyl p-tolyl sulfide µM µmol/L MTSO Methyl p-tolyl sulfoxide aa Amino acids MTSO2 Methyl p-tolyl sulfone + AGE Agarose gel electrophoresis NAD Nicotinamide adenine dinucleotide, oxidized aq. dest. Distilled water NADH Nicotinamide adenine dinucleotide, reduced + BLAST Basic Local Alignment Search NADP Nicotinamide adenine dinucleotide Tool phosphate, oxidized bp Base pair(s) NADPH Nicotinamide adenine dinucleotide phosphate, reduced BVMO Baeyer-Villiger monooxyge- OD600 Optical density at 600 nm nase CHMO Cyclohexanone monooxyge- PAGE Polyacrylamide gel electrophoresis nase Da Dalton PAMO Phenylacetone monooxygenase DMF Dimethyl formamide PCR Polymerase chain reaction DMSO Dimethyl sulfoxide PDB Protein Data Bank DMSO2 Dimethyl sulfone rpm Revolutions per minute DNA Desoxyribonucleic acid rv Reverse dNTP Desoxynucleoside triphosphate SDS Sodium dodecyl sulfate E. coli Escherichia coli SOC Super Optimal broth with Catabolite repression ee Enantiomeric excess TAE TRIS-Acetate-EDTA FAD Flavin adenine dinucleotide TB Terrific broth Fig. -
Phylogenetic and Taxonomic Position of the Genus Wollea with the Description of Wollea Salina Sp
Fottea, Olomouc, 16(1): 43–55, 2016 43 DOI: 10.5507/fot.2015.026 Phylogenetic and taxonomic position of the genus Wollea with the description of Wollea salina sp. nov. (Cyanobacteria, Nostocales) Eliška KozlíKová–zapomělová1, Thomrat CHATCHAWAN2, Jan KaštOVSKÝ3 & Jiří KOMÁREK3,4,* 1 Biology Centre of AS CR, Institute of Hydrobiology, Na Sádkách 7, CZ 37005 České Budějovice, Czech Re- public 2 Maejo University Phrae Campus, Mae Sai, Rong Kwang, 54140, Thailand 3 Department of Botany, Faculty of Science, University of South Bohemia, Branišovská 31, CZ–370 05 České Budějovice, Czech Republic 4 Institute of Botany AS CR and University of South Bohemia, Dukelská 135, CZ – 379 82 Třeboň, Czech Re- public; e–mail: [email protected] Abstract: The taxonomic separation of the related heterocytous cyanobacterial genera Wollea and Anabaena is unclear according to traditional taxonomic features, as modern polyphasic approach has not yet been applied to compare them. However, comparison of the type species of these genera and their polyphasic analyses enable the separation of both generic entities. Definitions of their diacritical characters follow from the combination of their phylogenetic and morphological criteria. The concepts of Anabaena sensu stricto (particularly without planktic types with gas vesicles in cells – Dolichospermum) and Wollea, derived from their types are proposed in the article and their review is presented in the table. A new species from saltworks in southern Thailand, W. salina, is described. Key words: Anabaena, Cyanobacteria, ecology, molecular analyses, morphology, polyphasic approach, taxonomy, Wollea INTRODUCTION larly with respect to molecular evaluation (16S rRNA gene sequences; zapomělová et al. 2013, in litt.). -
Genomic Analysis of Family UBA6911 (Group 18 Acidobacteria)
bioRxiv preprint doi: https://doi.org/10.1101/2021.04.09.439258; this version posted April 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 1 2 Genomic analysis of family UBA6911 (Group 18 3 Acidobacteria) expands the metabolic capacities of the 4 phylum and highlights adaptations to terrestrial habitats. 5 6 Archana Yadav1, Jenna C. Borrelli1, Mostafa S. Elshahed1, and Noha H. Youssef1* 7 8 1Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, 9 OK 10 *Correspondence: Noha H. Youssef: [email protected] bioRxiv preprint doi: https://doi.org/10.1101/2021.04.09.439258; this version posted April 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 11 Abstract 12 Approaches for recovering and analyzing genomes belonging to novel, hitherto unexplored 13 bacterial lineages have provided invaluable insights into the metabolic capabilities and 14 ecological roles of yet-uncultured taxa. The phylum Acidobacteria is one of the most prevalent 15 and ecologically successful lineages on earth yet, currently, multiple lineages within this phylum 16 remain unexplored. Here, we utilize genomes recovered from Zodletone spring, an anaerobic 17 sulfide and sulfur-rich spring in southwestern Oklahoma, as well as from multiple disparate soil 18 and non-soil habitats, to examine the metabolic capabilities and ecological role of members of 19 the family UBA6911 (group18) Acidobacteria. -
Additional Analysis of Cyanobacterial Polyamines Distributions Of
Microb. Resour. Syst. Dec.32(2 ):1792016 ─ 186, 2016 Vol. 32, No. 2 Additional analysis of cyanobacterial polyamines ─ Distributions of spermidine, homospermidine, spermine, and thermospermine within the phylum Cyanobacteria ─ Koei Hamana1)*, Takemitsu Furuchi2), Hidenori Hayashi1) and Masaru Niitsu2) 1)Faculty of Engineering, Maebashi Institute of Technology 460-1 Kamisadori-machi, Maebashi, Gunma 371-0816, Japan 2)Faculty of Pharmaceutical Sciences, Josai University, 1-1, Keyakidai, Sakado, Saitama 350-0295, Japan To further catalogue the distribution of cyanobacterial cellular polyamines, we used HPLC and HPGC to newly analyze the acid-extracted polyamines from 14 cyanobacteria. The colony-forming Nostoc verrucosum (“Ashitsuki”) and Nostoc commune (“Ishikurage”), as well as Anabaena species (Nostocales), contained homospermidine. The thermo-halotolerant Spirulina subsalsa var. salina (Spirulinales), as well as freshwater Spirulina strains, contained spermidine. Putrescine, spermidine, and homospermidine were found in freshwater colony-forming Aphanothece sacrum (“Suizenji-nori”), whereas the halotolerant Aphanothece halophytica and Microcystis species (Chroococcales) contained spermidine alone. In addition to putrescine, spermidine, homospermidine and agmatine, thermospermine was found as a major polyamine in haloalkaliphilic Arthrospira platensis (“Spirulina”) (Oscillatoriales). In the Synechococcales, chlorophyll b-containing Prochlorococcus marina contained spermidine, and chlorophyll d-containing Acaryochloris marina contained -
Cloning of Firefly Luciferase Cdna and the Expression of Active
Proc. Natl. Acad. Sci. USA Vol. 82, pp. 7870-7873, December 1985 Biochemistry Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli (bioluminescence/Photinus pyralis/antibody screening/expression vector/recombinant DNA) JEFFREY R. DE WET*, KEITH V. WOODt, DONALD R. HELINSKI*, AND MARLENE DELUCAt Departments of *Biology and tChemistry, University of California, San Diego, La Jolla, CA 92093 Communicated by W. D. McElroy, July 26, 1985 ABSTRACT A cDNA library was constructed from firefly library was screened with anti-P. pyralis luciferase antibody, (Photinuspyralis) lantern poly(A)I RNA, using the Escherichia using a chromogenic detection technique (8), and several coli expression vector Xgtll. The library was screened with cDNA clones were isolated and characterized. These clones anti-P. pyralis luciferase (Photinus luciferin:oxygen 4-oxidore- were found to be homologous to the mRNA that encodes ductase, EC 1.13.12.7) antibody, and several cDNA clones luciferase. The largest luciferase cDNA clone that was expressing luciferase antigens were isolated. One clone, ALucl, isolated was able to direct the synthesis of active luciferase contained 1.5 kilobase pairs of cDNA that hybridized to a 1.9- in E. coli. to 2.0-kilobase band on a nitrocellulose blot of electrophoreti- cally fractionated lantern RNA. Hybridization of the cloned MATERIALS AND METHODS cDNA to lantern poly(A)I RNA selected an RNA that directed the in vitro synthesis of a single polypeptide. This polypeptide Enzymes and Strains. Restriction endonucleases and E. coli comigrated with luciferase on NaDodSO4/PAGE and produced DNA polymerase I were purchased from New England bioluminescence upon the addition of luciferin and ATP. -
Bioluminescence Is Produced by a Firefly-Like Luciferase but an Entirely
www.nature.com/scientificreports OPEN New Zealand glowworm (Arachnocampa luminosa) bioluminescence is produced by a Received: 8 November 2017 Accepted: 1 February 2018 frefy-like luciferase but an entirely Published: xx xx xxxx new luciferin Oliver C. Watkins1,2, Miriam L. Sharpe 1, Nigel B. Perry 2 & Kurt L. Krause 1 The New Zealand glowworm, Arachnocampa luminosa, is well-known for displays of blue-green bioluminescence, but details of its bioluminescent chemistry have been elusive. The glowworm is evolutionarily distant from other bioluminescent creatures studied in detail, including the frefy. We have isolated and characterised the molecular components of the glowworm luciferase-luciferin system using chromatography, mass spectrometry and 1H NMR spectroscopy. The purifed luciferase enzyme is in the same protein family as frefy luciferase (31% sequence identity). However, the luciferin substrate of this enzyme is produced from xanthurenic acid and tyrosine, and is entirely diferent to that of the frefy and known luciferins of other glowing creatures. A candidate luciferin structure is proposed, which needs to be confrmed by chemical synthesis and bioluminescence assays. These fndings show that luciferases can evolve independently from the same family of enzymes to produce light using structurally diferent luciferins. Glowworms are found in New Zealand and Australia, and are a major tourist attraction at sites located across both countries. In contrast to luminescent beetles such as the frefy (Coleoptera), whose bioluminescence has been well characterised (reviewed by ref.1), the molecular details of glowworm bioluminescence have remained elusive. Tese glowworms are the larvae of fungus gnats of the genus Arachnocampa, with eight species endemic to Australia and a single species found only in New Zealand2. -
Biodiversity and Distribution of Cyanobacteria at Dronning Maud Land, East Antarctica
ACyctaan oBboatcatneriicaa eMasat lAacnittaarnctai c3a3. 17-28 Málaga, 201078 BIODIVERSITY AND DISTRIBUTION OF CYANOBACTERIA AT DRONNING MAUD LAND, EAST ANTARCTICA Shiv Mohan SINGH1, Purnima SINGH2 & Nooruddin THAJUDDIN3* 1National Centre for Antarctic and Ocean Research, Headland Sada, Vasco-Da-Gama, Goa 403804, India. 2Department of Biotechnology, Purvanchal University, Jaunpur, India. 3Department of Microbiology, Bharathidasan University, Tiruchirappalli – 620 024, Tamilnadu, India. *Author for correspondence: [email protected] Recibido el 20 febrero de 2008, aceptado para su publicación el 5 de junio de 2008 Publicado "on line" en junio de 2008 ABSTRACT. Biodiversity and distribution of cyanobacteria at Dronning Maud Land, East Antarctica.The current study describes the biodiversity and distribution of cyanobacteria from the natural habitats of Schirmacher land, East Antarctica surveyed during 23rd Indian Antarctic Expedition (2003–2004). Cyanobacteria were mapped using the Global Positioning System (GPS). A total of 109 species (91 species were non-heterocystous and 18 species were heterocystous) from 30 genera and 9 families were recorded; 67, 86 and 14 species of cyanobacteria were identified at altitudes of sea level >100 m, 101–150 m and 398–461 m, respectively. The relative frequency and relative density of cyanobacterial populations in the microbial mats showed that 11 species from 8 genera were abundant and 6 species (Phormidium angustissimum, P. tenue, P. uncinatum Schizothrix vaginata, Nostoc kihlmanii and Plectonema terebrans) could be considered as dominant species in the study area. Key words. Antarctic, cyanobacteria, biodiversity, blue-green algae, Schirmacher oasis, Species distribution. RESUMEN. Biodiversidad y distribución de las cianobacterias de Dronning Maud Land, Antártida Oriental. En este estudio se describe la biodiversidad y distribución de las cianobacterias presentes en los hábitats naturales de Schirmacher, Antártida Oriental, muestreados durante la 23ª Expedición India a la Antártida (2003-2004). -
Scholarworks@UNO
University of New Orleans ScholarWorks@UNO University of New Orleans Theses and Dissertations Dissertations and Theses Summer 8-4-2011 Identification and characterization of enzymes involved in the biosynthesis of different phycobiliproteins in cyanobacteria Avijit Biswas University of New Orleans, [email protected] Follow this and additional works at: https://scholarworks.uno.edu/td Part of the Biochemistry, Biophysics, and Structural Biology Commons Recommended Citation Biswas, Avijit, "Identification and characterization of enzymes involved in the biosynthesis of different phycobiliproteins in cyanobacteria" (2011). University of New Orleans Theses and Dissertations. 446. https://scholarworks.uno.edu/td/446 This Dissertation-Restricted is protected by copyright and/or related rights. It has been brought to you by ScholarWorks@UNO with permission from the rights-holder(s). You are free to use this Dissertation-Restricted in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s) directly, unless additional rights are indicated by a Creative Commons license in the record and/or on the work itself. This Dissertation-Restricted has been accepted for inclusion in University of New Orleans Theses and Dissertations by an authorized administrator of ScholarWorks@UNO. For more information, please contact [email protected]. Identification and characterization of enzymes involved in biosynthesis of different phycobiliproteins in cyanobacteria A Thesis Submitted to the Graduate Faculty of the University of New Orleans in partial fulfillment of the requirements for the degree of Doctor of Philosophy In Chemistry (Biochemistry) By Avijit Biswas B.S. -
DOMAIN Bacteria PHYLUM Cyanobacteria
DOMAIN Bacteria PHYLUM Cyanobacteria D Bacteria Cyanobacteria P C Chroobacteria Hormogoneae Cyanobacteria O Chroococcales Oscillatoriales Nostocales Stigonematales Sub I Sub III Sub IV F Homoeotrichaceae Chamaesiphonaceae Ammatoideaceae Microchaetaceae Borzinemataceae Family I Family I Family I Chroococcaceae Borziaceae Nostocaceae Capsosiraceae Dermocarpellaceae Gomontiellaceae Rivulariaceae Chlorogloeopsaceae Entophysalidaceae Oscillatoriaceae Scytonemataceae Fischerellaceae Gloeobacteraceae Phormidiaceae Loriellaceae Hydrococcaceae Pseudanabaenaceae Mastigocladaceae Hyellaceae Schizotrichaceae Nostochopsaceae Merismopediaceae Stigonemataceae Microsystaceae Synechococcaceae Xenococcaceae S-F Homoeotrichoideae Note: Families shown in green color above have breakout charts G Cyanocomperia Dactylococcopsis Prochlorothrix Cyanospira Prochlorococcus Prochloron S Amphithrix Cyanocomperia africana Desmonema Ercegovicia Halomicronema Halospirulina Leptobasis Lichen Palaeopleurocapsa Phormidiochaete Physactis Key to Vertical Axis Planktotricoides D=Domain; P=Phylum; C=Class; O=Order; F=Family Polychlamydum S-F=Sub-Family; G=Genus; S=Species; S-S=Sub-Species Pulvinaria Schmidlea Sphaerocavum Taxa are from the Taxonomicon, using Systema Natura 2000 . Triochocoleus http://www.taxonomy.nl/Taxonomicon/TaxonTree.aspx?id=71022 S-S Desmonema wrangelii Palaeopleurocapsa wopfnerii Pulvinaria suecica Key Genera D Bacteria Cyanobacteria P C Chroobacteria Hormogoneae Cyanobacteria O Chroococcales Oscillatoriales Nostocales Stigonematales Sub I Sub III Sub -
Efficiency of Partial 16S Rrna Gene Sequencing As Molecular Marker for Phylogenetic Study of Cyanobacteria, with Emphasis on Some Complex Taxa
Volume 61(1):59-68, 2017 Acta Biologica Szegediensis http://www2.sci.u-szeged.hu/ABS ARTICLE Efficiency of partial 16S rRNA gene sequencing as molecular marker for phylogenetic study of cyanobacteria, with emphasis on some complex taxa Zeinab Shariatmadari1*, Farideh Moharrek2, Hossein Riahi1, Fatemeh Heidari1, Elaheh Aslani1 1Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, G.C. Tehran, Iran 2Department of Plant Biology, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran ABSTRACT At present, the analysis of 16S rRNA gene sequences is the most commonly used KEY WORDS molecular marker for phylogenetic studies of cyanobacteria. However, in many studies partial cyanobacteria sequences is used. To evaluate the performance of this molecular marker, phylogenetic relation- intermixed taxa ship of several taxa from this phylum, especially some intermixed taxa, was studied. We analyzed molecular phylogeny a data set consisting of three categories of cyanobacterial strains, traditionally classified in three taxonomy orders, by morphological and phylogenetic analyses. The phylogenetic analyses were performed 16S rRNA gene with an emphasis on partial 16S rRNA gene sequences (600 bp) and the phylogenetic relation- ships were assessed using Maximum Parsimony, Maximum Likelihood and Bayesian Inference. In morphometric study, numerical taxonomy was performed on several morphospecies, and cluster analysis was performed using SPSS software. Based on the findings of this study, unlike the morphological analysis which was useful in several taxonomic ranks, this molecular marker is recommended for use only in high taxonomic levels such as order and family, because, contrary to our expectations, using partial 16S rRNA gene sequencing in the lower taxonomic levels, even in the genus level, was not necessarily successful. -
Supplementary Material the Metallochaperone Encoding Gene Hypa Is Widely Distributed Among Pathogenic Aeromonas Spp
Supplementary material The Metallochaperone Encoding Gene hypA Is Widely Distributed among Pathogenic Aeromonas spp. and Its Expression Is Increased under Acidic pH and within Macrophages. Ana Fernández-Bravo, Loida López-Fernández*, Maria José Figueras*. Unit of Microbiology, Department of Basic Health Sciences, Faculty of Medicine and Health Sciences, IISPV, University Rovira i Virgili, Reus, Spain. *Correspondence: Dr. Maria José Figueras, [email protected]; Dr. Loida López-Fernández, [email protected] Figure S1. Phylogenetic tree constructed with 25 species of Aeromonas based on sequences of the protein HypA by the Maximum- Likelihood algorithm (model JTT+G). Numbers at nodes denote the level of bootstrap based on 1000 replicates; only values greater than 50% are shown. Scale bar, base substitutions per site. 1 Table S1. Genetic analyses and diversity of hypA presence at strain-level in 143 genomes from 36 different species from the genus Aeromonas. T indicates type strain. Accesion number HypA Rate of hypA Species Strain Identified (NCBI) (genome) Re-identification Presence presence (%) CECT 4199 T A. allosaccharophila NZ_CDBR00000000.1 - Yes BVH88 A. allosaccharophila NZ_CDCB00000000.1 A. allosaccharophila Yes A. allosaccharophila 4/4 Z9-6 A. allosaccharophila NZ_NXBS00000000.1 A. allosaccharophila Yes (100) TTU2014- A. allosaccharophila NZ_CDCB00000000.1 A. allosaccharophila Yes 159ASC CECT 4227 T A. bestiarum NZ_CDDA00000000.1 - Yes A. bestiarum 2/2 CA23 Aeromonas sp. NZ_CP023818.1 A. bestiarum Yes 100 CECT 7113 T A. bivalvium NZ_CDBT00000000.1 - No ZJ19-2 A.bivalvium NZ_NXBQ00000000.1 A.bivalvium No 3/3 A. bivalvium 100 ZJ20-2 A.bivalvium NZ_NXBX00000000.1 A.bivalvium No CECT 838 T A.