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Peter Schonheit - One of the best experts on this subject based on the ideXlab platform.
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Thermostable Branched-Chain Amino Acid Transaminases From the Archaea Geoglobus acetivorans and Archaeoglobus fulgidus: Biochemical and Structural Characterization
Frontiers in bioengineering and biotechnology, 2019Co-Authors: Michail N. Isupov, Peter Schonheit, Konstantin M. Boyko, Jan-moritz Sutter, Paul James, C. Sayer, Marcel Schmidt, Alena Yu. Nikolaeva, T.n. Stekhanova, Andrey V. MardanovAbstract:Two new thermophilic branched chain amino acid transaminases have been identified within the genomes of different hyper-thermophilic archaea, Geoglobus acetivorans, and Archaeoglobus fulgidus. These enzymes belong to the class IV of transaminases as defined by their structural fold. The enzymes have been cloned and over-expressed in Escherichia coli and the recombinant enzymes have been characterized both biochemically and structurally. Both enzymes showed high thermostability with optimal temperature for activity at 80 and 85°C, respectively. They retain good activity after exposure to 50% of the organic solvents, ethanol, methanol, DMSO and acetonitrile. The enzymes show a low activity to (R)-methylbenzylamine but no activity to (S)-methylbenzylamine. Both enzymes have been crystallized and their structures solved in the internal aldimine form, to 1.9 A resolution for the Geoglobus enzyme and 2.0 A for the Archaeoglobus enzyme. Also the Geoglobus enzyme structure has been determined in complex with the amino acceptor α-ketoglutarate and the Archaeoglobus enzyme in complex with the inhibitor gabaculine. These two complexes have helped to determine the conformation of the enzymes during enzymatic turnover and have increased understanding of their substrate specificity. A comparison has been made with another (R) selective class IV transaminase from the fungus Nectria haematococca which was previously studied in complex with gabaculine. The subtle structural differences between these enzymes has provided insight regarding their different substrate specificities.
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complete genome sequence analysis of Archaeoglobus fulgidus strain 7324 dsm 8774 a hyperthermophilic archaeal sulfate reducer from a north sea oil field
Standards in Genomic Sciences, 2017Co-Authors: Nils-kåre Birkeland, Lianna Poghosyan, Anne Fiebig, Peter Schonheit, Hans-peter KlenkAbstract:Archaeoglobus fulgidus is the type species of genus Archaeoglobus Stetter 1998, a hyperthermophilic sulfate reducing group within the Archaeoglobi class of the euryarchaeota phylum. Members of this genus grow heterotrophically or chemolithoautotrophically with sulfate or thiosulfate as electron acceptors. Except for A. fulgidus strain 7324 and the candidate species “Archaeoglobus lithotrophicus”, which both originate from deep oil-fields, the other members of this genus have been recovered from marine hydrothermal systems. Here we describe the features of the A. fulgidus strain 7324 genome as compared to the A. fulgidus VC16 type strain. The 2.3 Mbp genome sequence of strain 7324 shares about 93.5% sequence identity with that of strain VC16T but is about 138 Kbp longer, which is mostly due to two large ‘insertions’ carrying one extra cdc6 (cell-cycle control protein 6) gene, extra CRISPR elements and mobile genetic elements, a high-GC ncRNA gene (hgcC) and a large number of hypothetical gene functions. A comparison with four other Archaeoglobus spp. genomes identified 1001 core Archaeoglobus genes and more than 2900 pan-genome orthologous genes.
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adp dependent 6 phosphofructokinase an extremely thermophilic non allosteric enzyme from the hyperthermophilic sulfate reducing archaeon Archaeoglobus fulgidus strain 7324
Extremophiles, 2004Co-Authors: Thomas Hansen, Peter SchonheitAbstract:The hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324 has been shown to degrade starch via glucose using a modified Embden-Meyerhof pathway. In this pathway phosphorylation of fructose-6-phosphate to fructose-1,6 bisphosphate is catalyzed by an ADP-dependent 6-phosphofructokinase (ADP-PFK), which was purified 1,800-fold to homogeneity. The enzyme is composed of 50 kDa subunits and is eluted from gel filtration as both a homotetramer and a homodimer. It had a temperature optimum at 85°C and showed significant thermostability up to 95°C. Kinetic constants were determined for both reaction directions at pH 6.6 and 80°C. Rate dependence for all substrates followed Michaelis Menten kinetics. The apparent K m for ADP and fructose-6-phosphate (forward reaction) was 0.6 mM and 2.2 mM, respectively; the apparent V max was 1,200 U/mg. ADP-PFK catalyzed in vitro the reverse reaction, with apparent K m for fructose-1,6-bisophosphate and AMP of 5.7 and 1.4 mM, respectively, and a V max value of 85 U/mg. The enzyme did not use ATP, PPi, or acetyl phosphate as phosphoryl donor and was highly specific for fructose-6-phosphate as substrate. The A. fulgidus ADP-PFK did not phosphorylate glucose and thus differs from the bifunctional ADP-PFK/GLK from Methanococcus jannaschii. Divalent cations were required for catalytic activity; Mg2+, which was most effective, could be partially replaced by Mn2+, Ni2+, and Co2+. Enzyme activity was not allosterically regulated by classical effectors of bacterial and eukaryal ATP-PFKs, such as ADP, AMP, phosphoenolpyruvate, or citrate. N-terminal amino acid sequence showed high similarity to known ADP-PFKs. In the genome of Archaeoglobus fulgidus strain VC 16, which is closely related to strain 7324, no homologous gene for ADP-PFK could be identified.
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ADP-dependent 6-phosphofructokinase, an extremely thermophilic, non-allosteric enzyme from the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324
Extremophiles, 2004Co-Authors: Thomas Hansen, Peter SchonheitAbstract:The hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324 has been shown to degrade starch via glucose using a modified Embden-Meyerhof pathway. In this pathway phosphorylation of fructose-6-phosphate to fructose-1,6 bisphosphate is catalyzed by an ADP-dependent 6-phosphofructokinase (ADP-PFK), which was purified 1,800-fold to homogeneity. The enzyme is composed of 50 kDa subunits and is eluted from gel filtration as both a homotetramer and a homodimer. It had a temperature optimum at 85°C and showed significant thermostability up to 95°C. Kinetic constants were determined for both reaction directions at pH 6.6 and 80°C. Rate dependence for all substrates followed Michaelis Menten kinetics. The apparent K _m for ADP and fructose-6-phosphate (forward reaction) was 0.6 mM and 2.2 mM, respectively; the apparent V _max was 1,200 U/mg. ADP-PFK catalyzed in vitro the reverse reaction, with apparent K _m for fructose-1,6-bisophosphate and AMP of 5.7 and 1.4 mM, respectively, and a V _max value of 85 U/mg. The enzyme did not use ATP, PPi, or acetyl phosphate as phosphoryl donor and was highly specific for fructose-6-phosphate as substrate. The A. fulgidus ADP-PFK did not phosphorylate glucose and thus differs from the bifunctional ADP-PFK/GLK from Methanococcus jannaschii . Divalent cations were required for catalytic activity; Mg^2+, which was most effective, could be partially replaced by Mn^2+, Ni^2+, and Co^2+. Enzyme activity was not allosterically regulated by classical effectors of bacterial and eukaryal ATP-PFKs, such as ADP, AMP, phosphoenolpyruvate, or citrate. N-terminal amino acid sequence showed high similarity to known ADP-PFKs. In the genome of Archaeoglobus fulgidus strain VC 16, which is closely related to strain 7324, no homologous gene for ADP-PFK could be identified.
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ADP-dependent glucokinase from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324.
Archives of microbiology, 2003Co-Authors: Antje Labes, Peter SchonheitAbstract:The hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324 has been shown to degrade starch via glucose using a modified Embden-Meyerhof pathway. The first enzyme of this pathway, ADP-dependent glucokinase, was purified 600-fold to homogeneity. The enzyme is a monomeric protein with an apparent molecular mass of 50 kDa. It had a temperature optimum at 83 °C and showed a significant thermostability up to 100 °C. The enzyme was highly specific for ADP and glucose as substrates; it did not use ATP, CDP, UDP, or GDP as phosphoryl donors, or mannose, fructose and fructose 6-phosphate as phosphoryl acceptors (at 80 °C). Only glucosamine was phosphorylated at significant rates. The apparent Km values for ADP and glucose (at 50 °C) were 0.07 mM and 0.78 mM, respectively; the apparent Vmax value was about 50 U/mg at 50 °C and 350 U/mg at 80 °C. Divalent cations were required for maximal activity; Mn2+, Mg2+ and Ca2+, which were most effective, could be replaced partially by Cu2+, Ni2+, Co2+ and Zn2+. The N-terminal amino acid sequence (42 amino acids) of ADP-dependent glucokinase was almost identical to that of ADP-dependent glucokinase from Thermococcus litoralis. In the genome of the closely related Archaeoglobus fulgidus strain VC16 a homologous gene for ADP-dependent glucokinase could not be identified.
Karl O Stetter - One of the best experts on this subject based on the ideXlab platform.
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Crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Archaeoglobus fulgidus.
Acta Crystallographica Section D Biological Crystallography, 2000Co-Authors: Annette Roth, Ulrich Ermler, Harald Huber, Karl O Stetter, Günther Fritz, Thomas Büchert, Peter M. H. KroneckAbstract:A group of anaerobic microorganisms use sulfate as the terminal electron acceptor for energy conservation. The process of sulfate reduction involves several enzymatic steps. One of them is the conversion of adenylyl sulfate (adenosine-5′-phosphosulfate) to sulfite, catalyzed by adenylylsulfate reductase. This enzyme is composed of a FAD-containing α-subunit and a β-subunit harbouring two [4Fe–4S] clusters. Adenylylsulfate reductase was isolated from Archaeoglobus fulgidus under anaerobic conditions and crystallized using the hanging-drop vapour-diffusion method using PEG 4000 as precipitant. The crystals grew in space group P212121, with unit-cell parameters a = 72.4, b = 113.2, c = 194.0 A. The asymmetric unit probably contains two αβ units. The crystals diffract beyond 2 A resolution and are suitable for X-ray structure analysis.
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Archaeoglobus veneficus sp. nov., a novel facultative chemolithoautotrophic hyperthermophilic sulfite reducer, isolated from abyssal black smokers
Systematic and Applied Microbiology, 1997Co-Authors: Harald Huber, Holger W Jannasch, Reinhard Rachel, Tanja Fuchs, Karl O StetterAbstract:Summary Four hyperthermophilic isolates of motile, highly irregular archaeal cocci were obtained from the walls of active “black smokers” at the Mid-Atlantic Ridge (depth 3500 meters). These obligate anaerobic organisms grew at temperatures between 65 °C and 85 °C (optimum 75 to 80 °C) at atmospheric pressure. Molecular hydrogen served as electron donor during chemolithoautotrophic growth and H 2 S was formed from sulfite or thiosulfate. Alternatively, organic acids, glucose, or ethanol were used as electron donors. Sulfate, nitrate, or nitrite could not serve as electron acceptors and elemental sulfur inhibited growth. The cells showed a blue-green fluorescence at 436 nm and produced small amounts of methane. One isolate (SNP6) was studied in detail. The G+C content of its DNA was 45 mol%. Based on DNA-DNA hybridization and 16S rDNA sequencing the new isolate was identified as a new species of the genus Archaeoglobus , which is named Archaeoglobus veneficus (type strain: SNP6; DSM 11195).
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N5,N10-methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri.
Archives of microbiology, 1993Co-Authors: Albrecht Klein, Karl O Stetter, J. Breitung, Dietmar Linder, Rudolf K. ThauerAbstract:Archaeoglobus fulgidus and Methanopyrus kandleri are both extremely thermophilic Archaea with a growth temperature optimum at 83°C and 98°C, respectively. Both Archaea contain an active N5,N10-methenyltetrahydromethanopterin cyclohydrolase. The enzyme from M. kandleri has recently been characterized. We describe here the purification and properties of the enzyme from A. fulgidus.
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Formylmethanofuran: tetrahydromethanopterin formyltransferase and N5,N10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea.
Archives of microbiology, 1993Co-Authors: Beatrix Schwörer, Karl O Stetter, Albrecht Klein, J. Breitung, Rudolf K. ThauerAbstract:The sulfate-reducing Archaeoglobus fulgidus contains a number of enzymes previously thought to be unique for methanogenic Archaea. The purification and properties of two of these enzymes, of formylmethanofuran: tetrahydromethanopterin formyltransferase and of N5,N10-methylenetetrahydromethanopterin dehydrogenase (coenzyme F420 dependent) are described here. A comparison of the N-terminal amino acid sequences and of other molecular properties with those of the respective enzymes from three methanogenic Archaea revealed a high degree of similarity.
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Formylmethanofuran: tetrahydromethanopterin formyltransferase and NS,N ~ dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea
1993Co-Authors: B. Schw, Karl O Stetter, Albrecht Klein, J. Breitung, Rudolf K. ThauerAbstract:The sulfate-reducing Archaeoglobus fulgidus contains a number of enzymes previously thought to be unique for methanogenic Archaea. The purification and properties of two of these enzymes, of formylmethanofu- ran:tetrahydrome thanopterin formyltransferase and of NS,N~ ~ dehydro- genase (coenzyme F42o dependent) are described here. A comparison of the N-terminal amino acid sequences and of other molecular properties with those of the respective enzymes from three methanogenic Archaea revealed a high degree of similarity.
Nils-kåre Birkeland - One of the best experts on this subject based on the ideXlab platform.
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complete genome sequence analysis of Archaeoglobus fulgidus strain 7324 dsm 8774 a hyperthermophilic archaeal sulfate reducer from a north sea oil field
Standards in Genomic Sciences, 2017Co-Authors: Nils-kåre Birkeland, Lianna Poghosyan, Anne Fiebig, Peter Schonheit, Hans-peter KlenkAbstract:Archaeoglobus fulgidus is the type species of genus Archaeoglobus Stetter 1998, a hyperthermophilic sulfate reducing group within the Archaeoglobi class of the euryarchaeota phylum. Members of this genus grow heterotrophically or chemolithoautotrophically with sulfate or thiosulfate as electron acceptors. Except for A. fulgidus strain 7324 and the candidate species “Archaeoglobus lithotrophicus”, which both originate from deep oil-fields, the other members of this genus have been recovered from marine hydrothermal systems. Here we describe the features of the A. fulgidus strain 7324 genome as compared to the A. fulgidus VC16 type strain. The 2.3 Mbp genome sequence of strain 7324 shares about 93.5% sequence identity with that of strain VC16T but is about 138 Kbp longer, which is mostly due to two large ‘insertions’ carrying one extra cdc6 (cell-cycle control protein 6) gene, extra CRISPR elements and mobile genetic elements, a high-GC ncRNA gene (hgcC) and a large number of hypothetical gene functions. A comparison with four other Archaeoglobus spp. genomes identified 1001 core Archaeoglobus genes and more than 2900 pan-genome orthologous genes.
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The pH optimum of native uracil-DNA glycosylase of Archaeoglobus fulgidus compared to recombinant enzyme indicates adaption to cytosolic pH.
Acta biochimica Polonica, 2014Co-Authors: Ingeborg Knævelsrud, Nils-kåre Birkeland, Sabina Kazazic, Svein BjellandAbstract:Uracil-DNA glycosylase of Archaeoglobus fulgidus (Afung) in cell extracts exhibited maximal activity around pH 6.2 as compared to pH 4.8 for the purified recombinant enzyme expressed in Escherichia coli. Native Afung thus seems to be adapted to the intracellular pH of A. fulgidus, determined to be 7.0±0.1. Both recombinant and native Afung exhibited a broad temperature optimum for activity around 80°C, reflecting the A. fulgidus optimal growth temperature of 83°C. Adaption to the neutral conditions in the A. fulgidus cytoplasm might be due to covalent modifications or accessory factors, or due to a different folding when expressed in the native host.
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Methylpurine DNA glycosylase of the hyperthermophilic archaeon Archaeoglobus fulgidus.
Biochemistry, 2002Co-Authors: Nils-kåre Birkeland, Ingeborg Knævelsrud, Hilde Ånensen, Wenche Kristoffersen, Magnar Bjørås, Frank T. Robb, And Arne Klungland, Svein BjellandAbstract:Base excision repair of DNA alkylation damage is initiated by a methylpurine DNA glycosylase (MPG) function. Such enzymes have previously been characterized from bacteria and eukarya, but not from archaea. We identified activity for the release of methylated bases from DNA in cell-free extracts of Archaeoglobus fulgidus, an archaeon growing optimally at 83 degrees C. An open reading frame homologous to the alkA gene of Escherichia coli was overexpressed and identified as a gene encoding an MPG enzyme (M(r) = 34 251), hereafter designated afalkA. The purified AfalkA protein differs from E. coli AlkA by excising alkylated bases only, from DNA, in the following order of efficiency: 3-methyladenine (m(3)A) >> 3-methylguanine approximately 7-methyladenine >> 7-methylguanine. Although the rate of enzymatic release of m(3)A is highest in the temperature range of 65-75 degrees C, it is only reduced by 50% at 45 degrees C, a temperature that does not support growth of A. fulgidus. At temperatures above 75 degrees C, nonenzymatic release of methylpurines predominates. The results suggest that the biological function of AfalkA is to excise m(3)A from DNA at suboptimal and maybe even mesophilic temperatures. This hypothesis is further supported by the observation that the afalkA gene function suppresses the alkylation sensitivity of the E. coli tag alkA double mutant. The amino acid sequence similarity and evolutionary relationship of AfalkA with other MPG enzymes from the three domains of life are described and discussed.
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[2] Isocitrate dehydrogenase, malate dehydrogenase, and glutamate dehydrogenase from Archaeoglobus fulgidus
Methods in enzymology, 2001Co-Authors: Ida Helene Steen, Torleiv Lien, Hilde Hvoslef, Nils-kåre BirkelandAbstract:Publisher Summary Archaeoglobus fulgidus is a hyperthermophilic sulfate-reducing archaeon belonging to the Euryarchaeota . Archaeoglobus fulgidus lacks a complete citric acid cycle, but the presence of enzymes required for the stepwise reductive formation of succinate from oxaloacetate and oxidative formation of 2-oxoglutarate from oxaloacetate and acetyl-CoA has been demonstrated, indicating the involvement of these enzymes in anabolism. Only two of these enzymes, isocitrate dehydrogenase (IDH) and malate dehydrogenase (MDH), have so far been purified and characterized. Glutamate dehydrogenase (GDH), which generally interconnects the citric acid cycle with nitrogen assimilation through a reductive amination of 2-oxogluarate to glutamate, is absent in the A. fulgidus type strain (VC-16), but has been purified from an oil-field isolate (strain 7324), in which it is an abundant protein. This article describes the purification and the catalytic and molecular properties of IDH, GDH, and MDH from A. fulgidus . Their thermostability is also compared. The similarity of the primary structures of IDH and MDH with those of corresponding enzymes from other organisms is discussed.
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Dissimilatory sulfite reductase from Archaeoglobus profundus and Desulfotomaculum thermocisternum : phylogenetic and structural implications from gene sequences
Extremophiles : life under extreme conditions, 1999Co-Authors: Øivind Larsen, Torleiv Lien, Nils-kåre BirkelandAbstract:The genes encoding the α- and β-subunits of dissimilatory sulfite reductase, dsrAB, from the hyper-thermophilic archaeon Archaeoglobus profundus and the thermophilic gram-positive bacterium Desulfotomaculum thermocisternum were cloned and sequenced. The dsrAB genes are contiguous, and most probably comprise an operon also including a dsrD homolog, a conserved gene of unknown function located downstream of dsrAB in all four sulfate reducers so far sequenced. Sequence comparison confirms that dissimilatory sulfite reductase, Dsr, is a highly conserved enzyme. A phylogenetic analysis using the available Dsr sequences, including Dsr-like proteins from nonsulfate reducers, suggests a paralogous origin of the α- and β-subunits. Furthermore, the Dsr from sulfate reducers forms a separate cluster, with Dsr from the bacterial sulfate reducers Desulfotomaculum thermocisternum and Desulfovibrio vulgaris branching together, next to Dsr from Archaeoglobus profundus and Archaeoglobus fulgidus. Based on an alignment with the assimilatory sulfite reductase from Escherichia coli, the amino acid residues involved in binding of sulfite, siroheme, and [Fe4S4]-clusters have been tentatively identified, which is consistent with the binding of two sirohemes and four [Fe4S4]-clusters per α2β2 structure. The evolution of Dsr and the structural basis for the binding of substrate and cofactors are discussed.
Koji Mori - One of the best experts on this subject based on the ideXlab platform.
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Archaeoglobus infectus sp nov a novel thermophilic chemolithoheterotrophic archaeon isolated from a deep sea rock collected at suiyo seamount izu bonin arc western pacific ocean
International Journal of Systematic and Evolutionary Microbiology, 2008Co-Authors: Koji Mori, Akihiko Maruyama, Tetsuro Urabe, Kenichiro Suzuki, Satoshi HanadaAbstract:A novel thermophilic, strictly anaerobic archaeon, designated strain Arc51T, was isolated from a rock sample collected from a deep-sea hydrothermal field in Suiyo Seamount, Izu-Bonin Arc, western Pacific Ocean. Cells of the isolate were irregular cocci with single flagella and exhibited blue–green fluorescence at 436 nm. The optimum temperature, pH and NaCl concentration for growth were 70 °C, pH 6.5 and 3 % (w/v), respectively. Strain Arc51T could grow on thiosulfate or sulfite as an electron acceptor in the presence of hydrogen. This strain required acetate as a carbon source for its growth, suggesting that the reductive acetyl CoA pathway for CO2 fixation was incomplete. In addition, coenzyme M (2-mercaptoethanesulfonic acid), which is a known methyl carrier in methanogenesis, was also a requirement for growth of the strain. Analysis of the 16S rRNA gene sequence revealed that the isolate was similar to members of the genus Archaeoglobus, with sequence similarities of 93.6–97.2 %; the closest relative was Archaeoglobus veneficus. Phylogenetic analyses of the dsrAB and apsA genes, encoding the alpha and beta subunits of dissimilatory sulfite reductase and the alpha subunit of adenosine-5′-phosphosulfate reductase, respectively, produced results similar to those inferred from comparisons based on the 16S rRNA gene sequence. On the basis of phenotypic and phylogenetic data, strain Arc51T represents a novel species of the genus Archaeoglobus, for which the name Archaeoglobus infectus sp. nov. is proposed. The type strain is Arc51T (=NBRC 100649T=DSM 18877T).
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Archaeoglobus infectus sp. nov., a novel thermophilic, chemolithoheterotrophic archaeon isolated from a deep-sea rock collected at Suiyo Seamount, Izu-Bonin Arc, western Pacific Ocean.
International journal of systematic and evolutionary microbiology, 2008Co-Authors: Koji Mori, Akihiko Maruyama, Tetsuro Urabe, Kenichiro Suzuki, Satoshi HanadaAbstract:A novel thermophilic, strictly anaerobic archaeon, designated strain Arc51T, was isolated from a rock sample collected from a deep-sea hydrothermal field in Suiyo Seamount, Izu-Bonin Arc, western Pacific Ocean. Cells of the isolate were irregular cocci with single flagella and exhibited blue-green fluorescence at 436 nm. The optimum temperature, pH and NaCl concentration for growth were 70 degrees C, pH 6.5 and 3 % (w/v), respectively. Strain Arc51T could grow on thiosulfate or sulfite as an electron acceptor in the presence of hydrogen. This strain required acetate as a carbon source for its growth, suggesting that the reductive acetyl CoA pathway for CO2 fixation was incomplete. In addition, coenzyme M (2-mercaptoethanesulfonic acid), which is a known methyl carrier in methanogenesis, was also a requirement for growth of the strain. Analysis of the 16S rRNA gene sequence revealed that the isolate was similar to members of the genus Archaeoglobus, with sequence similarities of 93.6-97.2 %; the closest relative was Archaeoglobus veneficus. Phylogenetic analyses of the dsrAB and apsA genes, encoding the alpha and beta subunits of dissimilatory sulfite reductase and the alpha subunit of adenosine-5'-phosphosulfate reductase, respectively, produced results similar to those inferred from comparisons based on the 16S rRNA gene sequence. On the basis of phenotypic and phylogenetic data, strain Arc51T represents a novel species of the genus Archaeoglobus, for which the name Archaeoglobus infectus sp. nov. is proposed. The type strain is Arc51T (=NBRC 100649T=DSM 18877T).
Satoshi Hanada - One of the best experts on this subject based on the ideXlab platform.
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Archaeoglobus infectus sp nov a novel thermophilic chemolithoheterotrophic archaeon isolated from a deep sea rock collected at suiyo seamount izu bonin arc western pacific ocean
International Journal of Systematic and Evolutionary Microbiology, 2008Co-Authors: Koji Mori, Akihiko Maruyama, Tetsuro Urabe, Kenichiro Suzuki, Satoshi HanadaAbstract:A novel thermophilic, strictly anaerobic archaeon, designated strain Arc51T, was isolated from a rock sample collected from a deep-sea hydrothermal field in Suiyo Seamount, Izu-Bonin Arc, western Pacific Ocean. Cells of the isolate were irregular cocci with single flagella and exhibited blue–green fluorescence at 436 nm. The optimum temperature, pH and NaCl concentration for growth were 70 °C, pH 6.5 and 3 % (w/v), respectively. Strain Arc51T could grow on thiosulfate or sulfite as an electron acceptor in the presence of hydrogen. This strain required acetate as a carbon source for its growth, suggesting that the reductive acetyl CoA pathway for CO2 fixation was incomplete. In addition, coenzyme M (2-mercaptoethanesulfonic acid), which is a known methyl carrier in methanogenesis, was also a requirement for growth of the strain. Analysis of the 16S rRNA gene sequence revealed that the isolate was similar to members of the genus Archaeoglobus, with sequence similarities of 93.6–97.2 %; the closest relative was Archaeoglobus veneficus. Phylogenetic analyses of the dsrAB and apsA genes, encoding the alpha and beta subunits of dissimilatory sulfite reductase and the alpha subunit of adenosine-5′-phosphosulfate reductase, respectively, produced results similar to those inferred from comparisons based on the 16S rRNA gene sequence. On the basis of phenotypic and phylogenetic data, strain Arc51T represents a novel species of the genus Archaeoglobus, for which the name Archaeoglobus infectus sp. nov. is proposed. The type strain is Arc51T (=NBRC 100649T=DSM 18877T).
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Archaeoglobus infectus sp. nov., a novel thermophilic, chemolithoheterotrophic archaeon isolated from a deep-sea rock collected at Suiyo Seamount, Izu-Bonin Arc, western Pacific Ocean.
International journal of systematic and evolutionary microbiology, 2008Co-Authors: Koji Mori, Akihiko Maruyama, Tetsuro Urabe, Kenichiro Suzuki, Satoshi HanadaAbstract:A novel thermophilic, strictly anaerobic archaeon, designated strain Arc51T, was isolated from a rock sample collected from a deep-sea hydrothermal field in Suiyo Seamount, Izu-Bonin Arc, western Pacific Ocean. Cells of the isolate were irregular cocci with single flagella and exhibited blue-green fluorescence at 436 nm. The optimum temperature, pH and NaCl concentration for growth were 70 degrees C, pH 6.5 and 3 % (w/v), respectively. Strain Arc51T could grow on thiosulfate or sulfite as an electron acceptor in the presence of hydrogen. This strain required acetate as a carbon source for its growth, suggesting that the reductive acetyl CoA pathway for CO2 fixation was incomplete. In addition, coenzyme M (2-mercaptoethanesulfonic acid), which is a known methyl carrier in methanogenesis, was also a requirement for growth of the strain. Analysis of the 16S rRNA gene sequence revealed that the isolate was similar to members of the genus Archaeoglobus, with sequence similarities of 93.6-97.2 %; the closest relative was Archaeoglobus veneficus. Phylogenetic analyses of the dsrAB and apsA genes, encoding the alpha and beta subunits of dissimilatory sulfite reductase and the alpha subunit of adenosine-5'-phosphosulfate reductase, respectively, produced results similar to those inferred from comparisons based on the 16S rRNA gene sequence. On the basis of phenotypic and phylogenetic data, strain Arc51T represents a novel species of the genus Archaeoglobus, for which the name Archaeoglobus infectus sp. nov. is proposed. The type strain is Arc51T (=NBRC 100649T=DSM 18877T).