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  • 1
    Electronic Resource
    Electronic Resource
    The gene encoding ammonia monooxygenase subunit A exists in three nearly identical copies in Nitrosospira sp. NpAV (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 139 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The gene encoding ammonia monooxygenase subunit A (AmoA) was found in three copies in the genome of the chemolithotrophic soil bacterium, Nitrosospira sp. NpAV. The open reading frame and flanking regions of the three copies were isolated from digested and size fractionated genomic DNA using oligodeoxyribonucleotide primers and polymerase chain reaction. The three gene copies of amoA were sequenced and the sequences compared to each other. The open reading frames and the upstream and downstream flanking regions were nearly identical in the three copies. All three copies were expressed in recombinant Escherichia coli strains from the indigenous promoter producing a product of approximately 30 kDa. All amoA copies encode 274 amino acid polypeptides which have similarity to the ammonia monooxygenase acetylene-binding protein from Nitrosomonas europaea.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08200.x
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of clade I catalases from Pseudomonas syringae and Listeria seeligeri (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1184-1186 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Haem-containing catalases are homotetrameric molecules that degrade hydrogen peroxide. Phylogenetically, the haem-containing catalases can be grouped into three main lines or clades. The crystal structures of seven catalases have been determined, all from clades II and III. In order to obtain a structure of an enzyme from clade I, which includes all plant, algae and some bacterial enzymes, two bacterial catalases, CatF from Pseudomonas syringae and Kat from Listeria seeligeri, have been crystallized by the hanging-drop vapour-diffusion technique, using PEG and ammonium sulfate as precipitants, respectively. Crystals of P. syringae CatF, with a plate-like morphology, belong to the monoclinic space group P21, with unit-cell parameters a = 60.6, b = 153.9, c = 109.2 Å, β = 102.8°. From these crystals a diffraction data set to 1.8 Å resolution with 98% completeness was collected using synchrotron radiation. Crystals of L. seeligeri Kat, with a well developed bipyramidal morphology, belong to space group I222 (or I212121), with unit-cell parameters a = 74.4, b = 121.3, c = 368.5 Å. These crystals diffracted beyond 2.2 Å resolution when using synchrotron radiation, but presented anisotropic diffraction, with the weakest direction perpendicular to the long c axis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901009817
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  • 3
    Electronic Resource
    Electronic Resource
    Multiple copies of ammonia monooxygenase (amo) operons have evolved under biased AT/GC mutational pressure in ammonia-oxidizing autotrophic bacteria (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 168 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The recent availability of complete sequences of ammonia monooxygenase (16 amoA, 5 amoB and 5 amoC gene sequences) and particulate methane monooxygenase (2 pmoA, pmoB and pmoC gene sequences each) genes allowed for a detailed analysis of their relatedness. Nucleotide sequence analysis was performed in order to identify the origins of the nearly identical operon copies within a given nitrosofier/methanotroph strain. Our data suggest that amo-homologous gene evolution has occurred in individual strains (orthology) under biased AT/GC pressure rather than by horizontal transfer. The multiple operon copies within individual strains are the result of operon duplication (paralogy). While the near identity of the multiple operon copies makes it impossible to determine whether paralogous gene expansion occurred in the last common ancestor of ammonia oxidizers or after speciation took place, we conclude that the duplication events were not recent events. We propose that the elimination of third basepair degeneracy between copies within one organism is implemented by a rectification mechanism resulting in concerted evolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13288.x
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  • 4
    Electronic Resource
    Electronic Resource
    A gene encoding a membrane protein exists upstream of the amoA/amoB genes in ammonia oxidizing bacteria: a third member of the amo operon? (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 150 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The gene cluster encoding ammonia monooxygenase (AMO) in the chemolithotrophic soil bacterium Nitrosospira sp. NpAV was found to contain a third open reading frame, termed amoC, upstream of the genes amoA and amoB that encode the subunits of AMO. The amoC gene and its flanking regions were isolated and sequenced from a 4.4 kb EcoRI fragment that contains one of three copies of the ammonia monooxygenase gene cluster. The presence of this gene upstream of the other two amoA gene copies in Nitrosospira NpAV as well as upstream of amoA genes in the genomes of other ammonia oxidizing nitrifiers (strains in the genera Nitrosomonas, Nitrosospira, Nitrosolobus and Nitrosovibrio) was confirmed using genomic DNA, oligodeoxyribonucleotide primers and the PCR. The amoC gene in Nitrosospira sp. NpAV encodes a 270 amino acid polypeptide of approximately 36 kDa. Topological analysis of the predicted primary structure revealed 6 membrane spanning domains. The amoC gene was expressed in recombinant Escherichia coli from its indigenous promoter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10351.x
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  • 5
    Electronic Resource
    Electronic Resource
    The amo operon in marine, ammonia-oxidizing γ-proteobacteria (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 180 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: While there is an extensive database of genes encoding ammonia monooxygenase (amo) found in the ammonia-oxidizing β-proteobacteria, few amo sequences are available representing the γ-proteobacteria. We sequenced the complete amo operon (amoCAB) for Nitrosococcus oceani (ATCC 19707), a marine, autotrophic, ammonia-oxidizing bacterium belonging to the γ-subdivision of the proteobacteria. An additional autotrophic, ammonia-oxidizing bacterium isolated from a marine environment (strain C-113) was identified as belonging to the Nitrosococcus genus by 16S rDNA analysis and its amo operon was sequenced. This is the first report of a full-length sequence for the amo operon from a γ-subdivision autotrophic ammonia-oxidizing bacterium. The N. oceani and C-113 amo genes were 88–90% identical to each other, 49–53% identical to the pmo genes encoding the related particulate methane monooxygenase of Methylococcus capsulatus (Bath), and 39–42% identical to the amo genes of the β-subdivision autotrophic ammonia-oxidizing bacteria. In both Nitrosococcus strains, the amo operon was found as a single copy and contained three genes, amoC, amoA, amoB, with intergenic spacer regions between amoC and amoA (286 bp) and between amoA and amoB (65 bp). We conclude that the amo genes will allow for a finer scale phylogenetic differentiation than 16S rDNA within the γ-subdivision AOB.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb08773.x
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  • 6
    Electronic Resource
    Electronic Resource
    The action of tentoxin on membrane processes in plants (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 74 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Tentoxin, a fungal phytotoxin, with its complex mode of action on plant membrane processes, is currently the best known example of a phytotoxic substance, with the literature going back more than 20 years and including a number of conflicting reports, which have not yet been adequately reconciled. This minireview covers all effects of tentoxin obtained at different levels of organization in several plant species (chloroplast structure and function, stomatal movements and guard cell protoplasts, leaf and root plasmalemma, ion uptake and translocation and internal ion concentrations) and suggests a number of targets for tentoxin which merit investigation. Besides the demonstration of the complexity of phytotoxin action and its possible relationship with other signal exchange mechanisms operating between microorganisms and plants, tentoxin may also provide a valuable tool for obtaining further information about the regulation of ion transport in plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb02021.x
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  • 7
    Electronic Resource
    Electronic Resource
    Growth and internal ion concentrations in seedlings of winter wheat are affected by 1 pM tentoxin (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 73 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The long-term effect of tentoxin on K+;, Ca2+ and total phosphorus (P) concentrations in the roots and shoots of 7- and 14-day-old seedlings of winter wheat (Triticum aestivum L. cv. Martonvásári-8) was studied. Growth (dry weight) and shoot to root ratios (dry weight and mineral concentrations) were also estimated. One pM tentoxin increased the shoot to root ratio for dry weight after a 14-day period of application. The concentration of Ca2+ slightly increased in the shoot. In roots, tentoxin caused a 30% higher accumulation of Ca2+ after 7 days, which did not change with treatment during the following 7 days. The accumulation of Ca2+ was enhanced by increasing concentrations of tentoxin. K+ and total P levels increased in roots but decreased in shoots after 7 days. However, they were redistributed between root and shoot during days 8–14 of tentoxin treatment. The effect of tentoxin is explained as a stimulation of ion transport mainly into the vacuoles of the immature metaxylem elements. It is suggested that tentoxin and other microbial products effective at very low concentrations may have a general significance in promoting plant infection or symbiosis via the modification of physiological or biochemical processes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb00600.x
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  • 8
    Electronic Resource
    Electronic Resource
    Effect of tentoxin on K+transport in winter wheat seedlings of different K+-status (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 72 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Klotz, M. G. and Erdei, L. 1988. Effect of tentoxin on K+ transport in winter wheat seedlings of different K+-status.The influence of the phytoeffective mycotoxin, tentoxin, [cyclo-(L-leucyl-N-methyltrans-dehydronhenyl-alanyl-glycyl-N-methyl-L-alanyl)] (in K+ uptake and on translocation of K+ from roots to shoot was studied in 14-day-old winter wheat plants (Triticum aestivum L. cv. Martonvásári-8) grown at different levels of K+ supply. For comparison, the effects of 2,4-dinilrophcnol and valinomycin were also investigated. In I-h experiments I pM tentoxin reduced K+ influx in the routs over the external K+ concentration range 0.1 to 1 mM (low-K+ plants), whereas stimulation was observed al lower and higher K+ concentrations. On the other hand, in plants grown at 0.3 mM K+, tentoxin stimulated the translocation of K+ from roots to shoots in 5-h experiments. Valinomycin affected K+ transport only al high K+-status (slight stimulation). In low-K+ plants 2,4-dinitrophenol (DNP) caused drastic inhibition of K+ uptake, but in high-K+ plants uptake was only slightly inhibited and translocation slightly stimulated, It is concluded that the opposite effects of tentoxin on K+ uptake and translocation agree1 with the directions of the H+-ATPases pumping H+ towards the apoplast and located at the cortex plasmalemma and the xylem parenchyma plasma-membrane, respectively. These effects should probably be attributed to the interaction between tentoxin and the K+-carrier protein rather than to a direct influence of tentoxin on H+-ATPase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb05836.x
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  • 9
    Electronic Resource
    Electronic Resource
    Picomolar concentrations of tentoxin affect Mg2+- and Ca2+-ATPase activities of plasma membrane vesicles from roots of winter wheat seedlings (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 75 (1989), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Purified plasmalemma vesicles were isolated in the presence of 250 mM sucrose from roots of 14-day-old seedlings of winter wheat (Triticum aestivum L. Martonvásári-8) by phase partitioning of salt-washed microsomal fractions in a Dextran-polyethylene glycol two-phase system, and both Mg2+- and Ca2+-ATPase activities were detected. Orthovanadate-sensitive Mg2+-ATPase activity associated with the inside of right side-out plasmalemma (PM) vesicles (latency 98%) was inhibited 76% by 0.3 mM Ca2+, Ca2+-dependent ATPase activity located partly on the inside and partly on the outside of plasmalemma vesicles (latency 47%) was not affected by Mg2+.Mg2+-ATPase activity was inhibited by 68% and inhibition of Mg2+ activation by 0.3 mM Ca2+ partly disappeared in the presence of 10 pM tentoxin, a fungal phytotoxin. Mg2+-ATPase activity remained inhibited up to 10 nM tentoxin while at 1 μM tentoxin Mg2+ activation was as high as without tentoxin. K+-stimulation and vanadate inhibition was increased and decreased, respectively, by 100 pM-10 nM tentoxin. Ca2+-dependent ATPase activity was continuously increased by 1 pM-10 nM tentoxin, but at 1 μM tentoxin the stimulation disappeared. The effects of pM tentoxin on plasma-lemma Mg2+-ATPase are discussed in relation to its influence on K+ transport in wheat seedlings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1989.tb04646.x
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  • 10
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    Addendum: Comparative genomic analysis of the class Epsilonproteobacteria and proposed reclassification to Epsilonbacteraeota (phyl. nov.) (2018)
    Frontiers Media
    Details
    Publication Date: 2022-05-25
    Description: © The Author(s), 2018. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Frontiers in Microbiology 9 (2018): 772, doi:10.3389/fmicb.2018.00772.
    Keywords: Epsilonproteobacteria ; Taxonomy ; Classification ; Genome ; Phylogenomics ; Epsilonbacteraeota ; Epsilonbacterota ; Evolution
    Repository Name: Woods Hole Open Access Server
    Type: Article
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