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Relevant bibliographies by topics / Methanothermobacter

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Academic literature on the topic 'Methanothermobacter'

Author: Grafiati

Published: 7 June 2025

Last updated: 26 June 2025

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Journal articles on the topic "Methanothermobacter"

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Liesegang, Heiko, Anne-Kristin Kaster, Arnim Wiezer, et al. "Complete Genome Sequence of Methanothermobacter marburgensis, a Methanoarchaeon Model Organism." Journal of Bacteriology 192, no. 21 (2010): 5850–51. http://dx.doi.org/10.1128/jb.00844-10.

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ABSTRACT The circular genome sequence of the chemolithoautotrophic euryarchaeon Methanothermobacter marburgensis, with 1,639,135 bp, was determined and compared with that of Methanothermobacter thermautotrophicus. The genomes of the two model methanogens differ substantially in protein coding sequences, in insertion sequence (IS)-like elements, and in clustered regularly interspaced short palindromic repeats (CRISPR) loci.

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Nakamura, Kohei, Takeshi Terada, Yuji Sekiguchi, et al. "Application of Pseudomurein Endoisopeptidase to Fluorescence In Situ Hybridization of Methanogens within the Family Methanobacteriaceae." Applied and Environmental Microbiology 72, no. 11 (2006): 6907–13. http://dx.doi.org/10.1128/aem.01499-06.

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ABSTRACT In situ detection of methanogens within the family Methanobacteriaceae is sometimes known to be unsuccessful due to the difficulty in permeability of oligonucleotide probes. Pseudomurein endoisopeptidase (Pei), a lytic enzyme that specifically acts on their cell walls, was applied prior to 16S rRNA-targeting fluorescence in situ hybridization (FISH). For this purpose, pure cultured methanogens within this family, Methanobacterium bryantii, Methanobrevibacter ruminantium, Methanosphaera stadtmanae, and Methanothermobacter thermautotrophicus together with a Methanothermobacter thermautotrophicus-containing syntrophic acetate-oxidizing coculture, endosymbiotic Methanobrevibacter methanogens within an anaerobic ciliate, and an upflow anaerobic sludge blanket (UASB) granule were examined. Even without the Pei treatment, Methanobacterium bryantii and Methanothermobacter thermautotrophicus cells are relatively well hybridized with oligonucleotide probes. However, almost none of the cells of Methanobrevibacter ruminantium, Methanosphaera stadtmanae, cocultured Methanothermobacter thermautotrophicus, and the endosymbiotic methanogens and the cells within UASB granule were hybridized. Pei treatment was able to increase the probe hybridization ratio in every specimen, particularly in the specimen that had shown little hybridization. Interestingly, the hybridizing signal intensity of Methanothermobacter thermautotrophicus cells in coculture with an acetate-oxidizing H2-producing syntroph was significantly improved by Pei pretreatment, whereas the probe was well hybridized with the cells of pure culture of the same strain. We found that the difference is attributed to the differences in cell wall thicknesses between the two culture conditions. These results indicate that Pei treatment is effective for FISH analysis of methanogens that show impermeability to the probe.

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Shima, Seigo, and Rudolf K. Thauer. "Methanothermobacter — Biokatalysator für die Energiewende." BIOspektrum 27, no. 1 (2021): 14–17. http://dx.doi.org/10.1007/s12268-021-1530-8.

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AbstractMethanothermobacter is a thermophilic genus within the kingdom of Euryarchaeota. Chemolithoautotrophic growth on H2 and CO2 at 65 °C is rapid and to high cell concentrations. Champions in this respect are the species M. thermautotrophicus and M. marburgensis, which were used to elucidate the unique biochemistry of methane formation from H2 and CO2. These two species are presently also being explored as biocatalysts in the industrial conversion of electrolytically produced H2 to “green” methane.

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Molitor, Bastian. "Genetischer Werkzeugkasten für Methanothermobacter thermautotrophicus." BIOspektrum 27, no. 1 (2021): 99. http://dx.doi.org/10.1007/s12268-021-1531-7.

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Engelhardt, Harald. "Methanothermobacter — bedeutungsvoll für Wasser, Energie, Klima." BIOspektrum 27, no. 1 (2021): 18–21. http://dx.doi.org/10.1007/s12268-021-1529-1.

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AbstractMethanogenic microbes live secretly in a kind of “parallel universe”, without light and oxygen. We can approach these microbes only by scientific means, but they are already of practical value for us and could — if we do not take care of efficient climate protection — even be of noticeable impact for our future world.

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Chen, Yen-Ju, Xiong Yu, Rajesh Kasiviswanathan, Jae-Ho Shin, Zvi Kelman, and Edward H. Egelman. "Structural Polymorphism of Methanothermobacter thermautotrophicus MCM." Journal of Molecular Biology 346, no. 2 (2005): 389–94. http://dx.doi.org/10.1016/j.jmb.2004.11.076.

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7

Nakamura, Kohei, Azumi Takahashi, Chikahiro Mori, et al. "Methanothermobacter tenebrarum sp. nov., a hydrogenotrophic, thermophilic methanogen isolated from gas-associated formation water of a natural gas field." International Journal of Systematic and Evolutionary Microbiology 63, Pt_2 (2013): 715–22. http://dx.doi.org/10.1099/ijs.0.041681-0.

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A thermophilic and hydrogenotrophic methanogen, strain RMAST, was isolated from gas-associated formation water of a gas-producing well in a natural gas field in Japan. Strain RMAST grew solely on H2/CO2 but required Casamino acids, tryptone, yeast extract or vitamins for growth. Growth of strain RMAST was stimulated by acetate. Cells were non-motile, straight rods (0.5×3.5–10.5 µm) and occurred singly or in pairs. Bundles of fimbriae occurred at both poles of cells and the cell wall was thick (approximately 21 nm, as revealed by ultrathin section electron microscopy). Strain RMAST grew at 45–80 °C (optimum, 70 °C), at pH 5.8–8.7 (optimum, pH 6.9–7.7) and with 0.001–20 g NaCl l−1 (optimum, 2.5 g NaCl l−1). Phylogenetic analysis revealed that Methanothermobacter thermautotrophicus ΔHT was most closely related to the isolate (95.7 % 16S rRNA gene sequence similarity). On the basis of morphological, phenotypic and phylogenetic characteristics, it is clear that strain RMAST represents a novel species of the genus Methanothermobacter , for which we propose the name Methanothermobacter tenebrarum sp. nov. The type strain is RMAST ( = DSM 23052T = JCM 16532T = NBRC 106236T).

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Wasserfallen, A., J. Nölling, P. Pfister, J. Reeve, and E. Conway de Macario. "Phylogenetic analysis of 18 thermophilic Methanobacterium isolates supports the proposals to create a new genus, Methanothermobacter gen. nov., and to reclassify several isolates in three species, Methanothermobacter thermautotrophicus comb. nov., Methanothermobacter wolfeii comb. nov., and Methanothermobacter marburgensis sp. nov." International Journal of Systematic and Evolutionary Microbiology 50, no. 1 (2000): 43–53. http://dx.doi.org/10.1099/00207713-50-1-43.

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Nagoya, Misa, Atsushi Kouzuma, Yoshiyuki Ueno, and Kazuya Watanabe. "Isolation of an Obligate Mixotrophic Methanogen That Represents the Major Population in Thermophilic Fixed-Bed Anaerobic Digesters." Microorganisms 8, no. 2 (2020): 217. http://dx.doi.org/10.3390/microorganisms8020217.

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Methanothermobacter Met2 is a metagenome-assembled genome (MAG) that encodes a putative mixotrophic methanogen constituting the major populations in thermophilic fixed-bed anaerobic digesters. In order to characterize its physiology, the present work isolated an archaeon (strain Met2-1) that represents Met2-type methanogens by using a combination of enrichments under a nitrogen atmosphere, colony formation on solid media and limiting dilution under high partial pressures of hydrogen. Strain Met2-1 utilizes hydrogen and carbon dioxide for methanogenesis, while the growth is observed only when culture media are additionally supplemented with acetate. It does not grow on acetate in the absence of hydrogen. The results demonstrate that Methanothermobacter sp. strain Met2-1 is a novel methanogen that exhibits obligate mixotrophy.

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Hassa, Julia, Daniel Wibberg, Irena Maus, Alfred Pühler, and Andreas Schlüter. "Genome Analyses and Genome-Centered Metatranscriptomics of Methanothermobacter wolfeii Strain SIV6, Isolated from a Thermophilic Production-Scale Biogas Fermenter." Microorganisms 8, no. 1 (2019): 13. http://dx.doi.org/10.3390/microorganisms8010013.

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In the thermophilic biogas-producing microbial community, the genus Methanothermobacter was previously described to be frequently abundant. The aim of this study was to establish and analyze the genome sequence of the archaeal strain Methanothermobacter wolfeii SIV6 originating from a thermophilic industrial-scale biogas fermenter and compare it to related reference genomes. The circular chromosome has a size of 1,686,891 bases, featuring a GC content of 48.89%. Comparative analyses considering three completely sequenced Methanothermobacter strains revealed a core genome of 1494 coding sequences and 16 strain specific genes for M. wolfeii SIV6, which include glycosyltransferases and CRISPR/cas associated genes. Moreover, M. wolfeii SIV6 harbors all genes for the hydrogenotrophic methanogenesis pathway and genome-centered metatranscriptomics indicates the high metabolic activity of this strain, with 25.18% of all transcripts per million (TPM) belong to the hydrogenotrophic methanogenesis pathway and 18.02% of these TPM exclusively belonging to the mcr operon. This operon encodes the different subunits of the enzyme methyl-coenzyme M reductase (EC: 2.8.4.1), which catalyzes the final and rate-limiting step during methanogenesis. Finally, fragment recruitment of metagenomic reads from the thermophilic biogas fermenter on the SIV6 genome showed that the strain is abundant (1.2%) within the indigenous microbial community. Detailed analysis of the archaeal isolate M. wolfeii SIV6 indicates its role and function within the microbial community of the thermophilic biogas fermenter, towards a better understanding of the biogas production process and a microbial-based management of this complex process.

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Dissertations / Theses on the topic "Methanothermobacter"

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McDermott, Paul B. "Proliferation mechanisms in Methanothermobacter thermautotrophicus DeltaH." Thesis, University of York, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.485452.

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Paras, Molly. "Multi-synthetase complex formation in methanothermobacter thermautotrophicus." Connect to resource, 2006. http://hdl.handle.net/1811/6509.

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Thesis (Honors)--Ohio State University, 2006.<br>Title from first page of PDF file. Document formatted into pages: contains 21 p.; also includes graphics. Includes bibliographical references (p. 20-21). Available online via Ohio State University's Knowledge Bank.

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Costa, Alessadro. "Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity." Thesis, Imperial College London, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.487549.

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The eukaryotic MCM2-7 replicative helicase is a hetero-oligomeric assembly comprising six .homologous polypeptides, which all belong to the superfamily of AAA+ ATPases (ATPases Associated vith various cellular Activities). The MCM complex works as a molecular motor which utilizes the energy produced by ATP hydrolysis to unwind the DNA double helix at the replication fork. Like most archaea, Methanothe.rmobacter thermautotrophicus possesses one copy of the MCM protein which forms a homo-oligomeric assembly and is used as a model for elucidating the mechanism of action of the eukaryotic homologue. Presented here is an electron-microscopy study of this archaeal MCM complex bound to different substrates. Although MCM is characterized by a high degree of polymorphism, I observed that hexameric configurations were.ÃƒÂƒ?ÃƒÂ‚Ã‚Â·stabilized upon DNA binding. I found that the DNA can interact with two distinct regions of the protein complex, either wrapping around the MCM ring, or threading through its central ch'annel. In particular, when treating the protein with a short stretch of DNA, a conformational change occurred within the ATPase domain, Teconfiguring the DNA interacting elements with'in the AAA+ module, which were found projecting inside the central channel of the MCM complex. In contrast, when treating the protein with longer stretches of DNA, the central channel was unoccupied and the DNA was found wrapped around the MCM ring in a configuration similar to that described for the bacterial DnaA initiator factor, an AAA+ ATPase involved in melting of the origin. The latter observation was unexpected and led to the jdef)tificationof a previously unrecognized helixturn- helix DNA binding motif within the outer belt of the MCM complex. Based on these observations I suggested that the MCM protein may have a dual role, contributing to origin melting during the initiation step, and acting as a canonical helicase at the replication fork during the elongation step of DNA replication.

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Gignac, Isabelle. "Protéomique structurale de Methanobacterium thermoautotrophicum; structure et fonction d'une protéine classifiée préservée dans le génome." Thesis, Université Laval, 2004. http://www.theses.ulaval.ca/2004/21738/21738.pdf.

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La fonction d’une protéine est ultimement déterminée par sa structure tridimensionnelle. La compréhension complète de la fonction d’une protéine implique donc la connaissance de sa structure. Le grand nombre de projet de séquençage de génome résulte en plusieurs dizaines de milliers de séquences de protéines pour lesquelles il n’existe aucune information fonctionnelle. La protéomique structurale implique l’étude de la structure tridimensionnelle de toutes les protéines d’un protéome. Comme la détermination de la structure d’une protéine est un processus laborieux, la protéomique structurale est un des plus grands défis scientifiques du 21e siècle. Malgré cela, plusieurs projets de protéomique structurale ont récemment débuté à travers le monde. Ce mémoire présente une étude qui s’inscrit dans le cadre d’un de ces projets à grande échelle, la protéomique structurale de Methanobacterium thermoautotrophicum. À l’aide de la résonance magnétique nucléaire, la structure tridimensionnelle de MTH187, une protéine de Methanobacterium thermoautotrophicum, a été déterminée. MTH187 est classifié comme ayant une séquence conservée, et sa fonction est inconnue. La structure de MTH187 révèle que cette protéine de 111 acides aminés est composée de six hélices α de 10 à 14 résidus. Par homologie structurale, il a été possible de classifier MTH187 parmi une famille structurale de type « HEAT repeat ». Les protéines de cette famille possèdent une fonction de reconnaissance protéines-protéines.

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Sakakibara, Nozomi. "Biochemical characterization of the Minichromosome maintenance (MCM) helicase from (Methanothermobacter thermautotrophicus)." College Park, Md. : University of Maryland, 2009. http://hdl.handle.net/1903/9238.

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Thesis (Ph. D.)--University of Maryland, College Park, 2009.<br>Thesis research directed by: Dept. of Chemistry and Biochemistry. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.

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Khandekar, Sanjay S. "Purification and characterization of fumarate reductase from Methanobacterium thermoautotrophicum." PDXScholar, 1986. https://pdxscholar.library.pdx.edu/open_access_etds/490.

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Anaerobic fermentation has been an established technology ever since man started treating sewage. Recently this process has received increased attention because of its inherent ability to produce methane gas, which apart from solar energy, is the cleanest, most non-polluting source of energy. Methanobacterium thermoautotrophicum, a thermophilic bacterium, grows on CO(,2) as a source of carbon as well as electron acceptor, using hydrogen as an electron donor. Labeling studies carried out with ('14)C have shown a presence of partial reductive TCA cycle. In this work, the enzyme fumarate reductase, which belongs to this cycle, has been purified to homogeneity using various separation techniques. In keeping with the thermophilic character of the organism, fumarate reductase is extremely heat resistant. Incubation at 75(DEGREES)C for 24 hours led to an increase in purification. In contrast, the enzyme was found to be very sensitive to oxygen. The crude extract, when exposed to air, lost half of its activity within 20 minutes. Reducing agents were helpful in protecting against loss of enzymatic activity provided that a strict anaerobic atmosphere was maintained. For this reason, the entire purification was performed inside a Freter-type anaerobic chamber using reducing agents. The molecular weight of the native fumarate reductase, as determined by Sephacryl S-300 gel exclusion chromatography, was found to be approximately 80,000. SDS polyacrylamide gel electrophoresis data suggested that the enzyme is a tetramer. Treatment with sulfhydyl reagents as well as Cu('++) caused loss in fumarate reductase activity, indicating that the enzyme contains at least one sulfhydryl group which is important to its activity. The UV/Visible spectrum of fumarate reductase did not reveal the presence of a flavin moiety as a cofactor. Both UV/Visible and fluorescence spectra of fumarate reductase from M. thermoautotrophicum instead, indicated the presence of an unusual cofactor, which could be similar to either tetrahydromethanopterin or F(,420).

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Sarbu, Christina [Verfasser], and Reinhard [Akademischer Betreuer] Wirth. "Untersuchung der Mth60-Fimbrien von Methanothermobacter thermoautotrophicus / Christina Sarbu. Betreuer: Reinhard Wirth." Regensburg : Universitätsbibliothek Regensburg, 2013. http://d-nb.info/1034758616/34.

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Kasiviswanathan, Rajesh. "Structural and functional analysis of dna replication initiation proteins from the archaeon methanothermobacter thermautotrophicus." College Park, Md. : University of Maryland, 2005. http://hdl.handle.net/1903/3152.

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Thesis (Ph. D.) -- University of Maryland, College Park, 2005.<br>Thesis research directed by: Cell Biology & Molecular Genetics. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.

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Boomershine, William P. "Structure and interactions of archaeal RNase P proteins Mth Rpp29 and Pfu Rpp21." Connect to this title online, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1117552357.

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Thesis (Ph. D.)--Ohio State University, 2005.<br>Title from first page of PDF file. Document formatted into pages; contains xv, 176 p.; also includes graphics Includes bibliographical references (p. 167-176). Available online via OhioLINK's ETD Center

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Yang, Na Duin Evert C. "Activation and inhibitor studies on methyl-coenzyme M reductase and purification of a new hydroxylamine oxidoreductase from methylomicrobium Album ATCC 33003." Auburn, Ala, 2008. http://repo.lib.auburn.edu/2007%20Fall%20Dissertations/Yang_Na_16.pdf.

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Books on the topic "Methanothermobacter"

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Luo, Yonkneng. Molecular Evolutionary Relationships among Extrachromosomal Elements in Methanothermobacter Strains. 2000.

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Book chapters on the topic "Methanothermobacter"

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Fink, Christian, Largus T. Angenent, and Bastian Molitor. "An Interdomain Conjugation Protocol for Plasmid-DNA Transfer into Methanothermobacter thermautotrophicus ΔH." In Archaea. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2445-6_7.

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Duin, Evert C., Divya Prakash, and Charlene Brungess. "Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis." In Methods in Methane Metabolism, Part A. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-12-385112-3.00009-3.

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Mühling, Lucas, Tina Baur, and Bastian Molitor. "Methanothermobacter thermautotrophicus and Alternative Methanogens: Archaea-Based Production." In Advances in Biochemical Engineering/Biotechnology. Springer Berlin Heidelberg, 2024. http://dx.doi.org/10.1007/10_2024_270.

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Xie, Yunwei, and John N. Reeve. "In Vitro Transcription Assays Using Components from Methanothermobacter thermautotrophicus." In Methods in Enzymology. Elsevier, 2003. http://dx.doi.org/10.1016/s0076-6879(03)70006-8.

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Prathiviraj, R., Sheela Berchmans, and P. Chellapandi. "Comparative Prediction of Electrical Interplay Systems in Methanothermobacter thermautotrophicus ΔH and Metal-loving Bacteria." In Marvels of Artificial and Computational Intelligence in Life Sciences. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815136807123010020.

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Bioelectrochemical technology has been developed to elucidate the mechanisms of electrical interplay systems for electromethanogenesis in microbial electrolysis cells (MEC). In the present study, we evaluated the electrical interplay systems for electromethanogenesis in Methanothermobacter thermautotrophicus ΔH (MTH). The modular structure of its protein-protein interaction (PPI) network was compared with the electrical interplay systems of metal-loving eubacteria (Geobacter metallireducens and G. sulfurreducens). The structure-function-metabolism link of each protein pair was evaluated to mine experimental PPI information from the literature. The results of our study indicate that the topological properties of the PPI networks are robust and consistent for sharing homologous protein interactions across metal-loving eubacteria. A large fraction of genes and associated PPI networks were established in the MTH for direct interspecies electron transfer systems, which were divergent from metal-loving eubacteria. MTH is predicted to generate CH4 by reducing CO2 with hydrogen in the geothermal environment through growth-associated electromethanogenesis. Thus, the present computational study will facilitate an understanding of the proteomic contexts and mechanisms of interspecies electron transfer between thermophilic autotrophic methanogenic archaea and metal-loving Eubacteria for electromethanogenesis.

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