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Dissertations / Theses on the topic 'Methanothermobacter'

Author: Grafiati

Published: 7 June 2025

Last updated: 26 June 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Xie, Yunwei. "Nucleosomes, transcription and transcription regulation in Archaea." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1127830717.

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Thesis (Ph. D.)--Ohio State University, 2005.<br>Title from first page of PDF file. Document formatted into pages; contains xiv, 200 p.; also includes graphics (some col.). Includes bibliographical references (p. 167-197). Available online via OhioLINK's ETD Center

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12

Vitt, Stella [Verfasser], and Seigo [Akademischer Betreuer] Shima. "Cryo-Elektronenmikroskopie- und Kristallstruktur der F420-reduzierenden [NiFe]-Hydrogenase (FrhABG) aus Methanothermobacter marburgensis / Stella Vitt. Betreuer: Seigo Shima." Marburg : Philipps-Universität Marburg, 2014. http://d-nb.info/1051934397/34.

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13

Ruth-Sarah, Rose. "An investigative study into the biosynthesis of coenzyme Fâ‚„â‚ƒâ‚€ Methanothermobacter thermoautotrophicus str. H and Methanosarcina barkeri str. Fusaro." Thesis, Queen Mary, University of London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.430454.

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14

Baumann, Lydia [Verfasser], and Jörn [Akademischer Betreuer] Peckmann. "Membrane lipids of the (hyper)thermophilic, methanogenic archaea Methanothermobacter marburgensis, Methanocaldococcus villosus and Methanothermococcus okinawensis and their geobiological and astrobiological relevance / Lydia Baumann ; Betreuer: Jörn Peckmann." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2020. http://d-nb.info/121390126X/34.

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15

Roy, Sébastien. "Étude de l'immobilisation d'une anhydrase carbonique (MTCA) thermostable de Methanobacterium thermoautotrophicum : effet de la séquestration dans un réseau poreux de silice sur la thermorésistance." Thesis, Université Laval, 2007. http://www.theses.ulaval.ca/2007/24174/24174.pdf.

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16

Barnes, Jeffrey Paul. "Is Mth1483p a subunit of RNase P in Methanothermobacter thermoautotrophicus?" 2004. http://www.lib.ncsu.edu/theses/available/etd-12012004-143203/unrestricted/etd.pdf.

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17

Ciirdaeva, Elena. "Investigations into the mode of action of the DNA uridine endonuclease Mth212 of Methanothermobacter thermautotrophicus ΔH". Doctoral thesis, 2010. http://hdl.handle.net/11858/00-1735-0000-0006-AD99-3.

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18

Schomacher, Lars. "Ein neu entdeckter Weg der Reparatur hydrolytisch geschädigter DNA-Cytosinreste, etabliert im thermophilen Archaeon Methanothermobacter thermautotrophicus ΔH". Doctoral thesis, 2007. http://hdl.handle.net/11858/00-1735-0000-000D-F230-F.

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19

Schomacher, Lars [Verfasser]. "Ein neu entdeckter Weg der Reparatur hydrolytisch geschädigter DNA-Cytosinreste, etabliert im thermophilen Archaeon Methanothermobacter thermautotrophicus ΔH [Delta-H] / vorgelegt von Lars Schomacher". 2007. http://d-nb.info/990198189/34.

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20

Ciirdaeva, Elena [Verfasser]. "Investigations into the mode of action of the DNA uridine endonuclease Mth212 of Methanothermobacter thermautotrophicus ΔH [Delta-H] / vorgelegt von Elena Ciirdaeva (geb. Jivotovscaia)". 2009. http://d-nb.info/100951394X/34.

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