Relevant bibliographies by topics / Selenomonas ruminantium

Academic literature on the topic 'Selenomonas ruminantium'

Author: Grafiati
Published: 4 June 2021
Last updated: 28 January 2023

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Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Journal articles on the topic "Selenomonas ruminantium":

1

Michel, Tomas A., and Joan M. Macy. "Ferredoxin from Selenomonas ruminantium." Archives of Microbiology 153, no. 5 (April 1990): 518–20. http://dx.doi.org/10.1007/bf00248437.

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2

Kalmokoff, M. L., J. W. Austin, M. F. Whitford, and R. M. Teather. "Characterization of a major envelope protein from the rumen anaerobeSelenomonas ruminantiumOB268." Canadian Journal of Microbiology 46, no. 4 (April 1, 2000): 295–303. http://dx.doi.org/10.1139/w99-149.

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Cell envelopes from the Gram-negative staining but phylogenetically Gram-positive rumen anaerobe Selenomonas ruminantium OB268 contained a major 42 kDa heat modifiable protein. A similarly sized protein was present in the envelopes of Selenomonas ruminantium D1 and Selenomonas infelix. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of Triton X-100 extracted cell envelopes from S. ruminantium OB268 showed that they consisted primarily of the 42 kDa protein. Polyclonal antisera produced against these envelopes cross-reacted only with the 42 kDa major envelope proteins in both S. ruminantium D1 and S. infelix, indicating a conservation of antigenic structure among each of the major envelope proteins. The N-terminus of the 42 kDa S. ruminantium OB268 envelope protein shared significant homology with the S-layer (surface) protein from Thermus thermophilus, as well as additional envelope proteins containing the cell surface binding region known as a surface layer-like homologous (SLH) domain. Thin section analysis of Triton X-100 extracted envelopes demonstrated the presence of an outer bilayer overlaying the cell wall, and a regularly ordered array was visible following freeze-fracture etching through this bilayer. These findings suggest that the regularly ordered array may be composed of the 42 kDa major envelope protein. The 42 kDa protein has similarities with regularly ordered outer membrane proteins (rOMP) reported in certain Gram-negative and ancient eubacteria.Key words: Selenomonas envelope surface SLH domain.
3

Pristas, Peter, and Maria Piknova. "Underrepresentation of short palindromes in Selenomonas ruminantium DNA: evidence for horizontal gene transfer of restriction and modification systems?" Canadian Journal of Microbiology 51, no. 4 (April 1, 2005): 315–18. http://dx.doi.org/10.1139/w05-004.

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Molecular analysis of isolates of the rumen bacterium Selenomonas ruminantium revealed a high variety and frequency of site-specific (restriction) endonucleases. While all known S. ruminantium restriction and modification systems recognize hexanucleotide sequences only, consistently low counts of both 6-bp and 4-bp palindromes were found in DNA sequences of S. ruminantium. Statistical analysis indicated that there is some correlation between the degree of underrepresentation of tetranucleotide words and the number of known restriction endonucleases for a given sequence. Control analysis showed the same correlation in lambda DNA but not in human adenovirus DNA. Based on the data presented, it could be proposed that there is a much higher historical occurrence of restriction and modification systems in S. ruminantium and (or) frequent horizontal gene transfer of restriction and modification gene complexes.Key words: Selenomonas, palindromes, restriction-modification.
4

Wiryawan, KG, and JD Brooker. "Probiotic control of lactate accumulation in acutely grain-fed sheep." Australian Journal of Agricultural Research 46, no. 8 (1995): 1555. http://dx.doi.org/10.1071/ar9951555.

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When sheep were acutely fed a grain diet, ruminal pH rapidly dropped to less than 5.0, lactic acid exceeded 100 mM and clinical symptoms of acidosis were evident within 24 h. When acute grain feeding was preceeded by inoculation of the rumen with 108 cfu of Selenomonas ruminantium subsp. lactilytica strain JDB201, ruminal lactate was undetectable and ruminal pH was stabilized at 6.3-6.5 for up to 24 h. Inoculation of the rumen with a mixture of 108 cfu each of Selenomonas ruminantium subsp. lactilytica strain JDB201 and Megasphaera elsdenii strain JDB301 was shown to be more effective than Selenomonas ruminantium subsp. lactilytica alone and maintained ruminal stability following acute grain feeding for up to 4 days. A continuous culture model of acidosis was also developed to test the effect of probiotic inoculation in combination with 0.75 8g/mL of Virginiamycin in preventing lactate accumulation and establishing a stable fermentation in vitro. The data suggest that although probiotic treatment is effective, a combination of probiotic and antibiotic may be the best approach to achieve rapid ruminal adaptation during acute grain feeding of sheep.
5

Haya, Shohei, Yuya Tokumaru, Naoki Abe, Jun Kaneko, and Shin-ichi Aizawa. "Characterization of Lateral Flagella of Selenomonas ruminantium." Applied and Environmental Microbiology 77, no. 8 (February 18, 2011): 2799–802. http://dx.doi.org/10.1128/aem.00286-11.

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ABSTRACTSelenomonas ruminantiumproduces a tuft of flagella near the midpoint of the cell body and swims by rotating the cell body along the cell's long axis. The flagellum is composed of a single kind of flagellin, which is heavily glycosylated. The hook length ofS. ruminantiumis almost double that ofSalmonella.
6

Fecskeová, Lívia, Peter Pristaš, and Peter Javorský. "Cloning and characterization of cobA, one of vitamin B12 biosynthesis pathway genes from Selenomonas ruminantium." Nova Biotechnologica et Chimica 10, no. 2 (August 31, 2021): 131–35. http://dx.doi.org/10.36547/nbc.1122.

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Bacterial biosynthesis of vitamin B12 can occur via either aerobic or anaerobic route. While the aerobic pathway has been fully elucidated and understood, less is known about the anaerobic pathway. Selenomonas ruminantium is thought to be the main producer of this vitamin in rumen environment and must use the anaerobic pathway. In our work we found one of the genes of vitamin B12 biosynthetic pathway of S. ruminantium, encoding for the cobalamin adenosyltransferase, enzyme taking part at the last steps of the synthesis process. Deduced amino acid sequence showed the highest similarity to cobalamin adenosyltransferases of other ruminal anaerobic bacteria and that of species Selenomonas. Phylogenetic comparisons of CobA protein sequences of several anaerobic bacteria of Clostridiale order indicate possible horizontal transfer of this gene.
7

Nisbet, David J., and Scott A. Martin. "Factors affecting L-lactate utilization by Selenomonas ruminantium." Journal of Animal Science 72, no. 5 (May 1, 1994): 1355–61. http://dx.doi.org/10.2527/1994.7251355x.

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8

Williams, D. K., and S. A. Martin. "Xylose uptake by the ruminal bacterium Selenomonas ruminantium." Applied and Environmental Microbiology 56, no. 6 (1990): 1683–88. http://dx.doi.org/10.1128/aem.56.6.1683-1688.1990.

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9

Brooker, J. D., and B. Stokes. "Monoclonal antibodies against the ruminal bacterium Selenomonas ruminantium." Applied and Environmental Microbiology 56, no. 7 (1990): 2193–99. http://dx.doi.org/10.1128/aem.56.7.2193-2199.1990.

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10

Kopecny, J., V. Kostyukovsky, and K. Fliegerova. "Electroporation of G+ host plasmids into Selenomonas ruminantium." CrossRef Listing Of Deleted DOIs 45, Suppl. 1 (1996): 356. http://dx.doi.org/10.1051/rnd:19960685.

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More sources
You might also be interested in the extended bibliographies on the topic 'Selenomonas ruminantium' for particular source types:
Journal articles

Dissertations / Theses on the topic "Selenomonas ruminantium":

1

Cheong, Judy Poh Eng. "Characterisation of a temperate bacteriophage of the ruminal bacterium Selenomonas ruminantium." Title page, contents and summary only, 1997. http://web4.library.adelaide.edu.au/theses/09PH/09phc5185.pdf.

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2

Gilmour, Martin. "Lactate utilisation in the rumen bacterium Selenomonas ruminantium." Thesis, Heriot-Watt University, 1994. http://hdl.handle.net/10399/1379.

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3

Zhang, Ning. "Molecular characterization of the ruminal bacterial species Selenomonas ruminantium : a thesis submitted to the University of Adelaide for the degree of Doctor of Philosophy /." Title page, contents and abstract only, 1992. http://web4.library.adelaide.edu.au/theses/09PH/09phn714.pdf.

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Thesis (Ph.D.)--University of Adelaide, Dept. of Animal Science, Waite Agricultural Research Institute, 1993.
Includes two of author's articles in pocket inside back cover. Includes bibliographical references (leaves 133-150).
4

Robertson, J. D. "The energetics of end product excretion from a rumen bacterium, Selenomonas ruminantium." Thesis, University of Aberdeen, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.373190.

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5

Ricke, Steven Clarence. "Characterization of hen egg yolk antibodies made to Selenomonas ruminantium, and growth and metabolic response of Selenomonas ruminantium HD₄ in high concentrations of ammonia." 1989. http://catalog.hathitrust.org/api/volumes/oclc/22269780.html.

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Thesis (Ph. D.)--University of Wisconsin--Madison, 1989.
Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
6

Zhang, Ning 1965. "Molecular characterization of the ruminal bacterial species Selenomonas ruminantium : a thesis submitted to the University of Adelaide for the degree of Doctor of Philosophy." 1992. http://web4.library.adelaide.edu.au/theses/09PH/09phn714.pdf.

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Includes two of author's articles in pocket inside back cover. Includes bibliographical references (leaves 133-150) Diversity in the ruminal Gram negative bacterial species Selenomonas ruminantium has been investigated by DNA fingerprinting, DNA homology and plasmid profile analysis. Twenty different isolates from the sheep rumen were classified morphologically and by carbon source utilization.
7

Zhang, Ning 1965. "Molecular characterization of the ruminal bacterial species Selenomonas ruminantium / by Zhang Ning." Thesis, 1992. http://hdl.handle.net/2440/21665.

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Abstract:
Includes two of author's articles in pocket inside back cover.
Includes bibliographical references (leaves 133-150)
xii, 150 leaves : ill. ; 30 cm.
Diversity in the ruminal Gram negative bacterial species Selenomonas ruminantium has been investigated by DNA fingerprinting, DNA homology and plasmid profile analysis. Twenty different isolates from the sheep rumen were classified morphologically and by carbon source utilization.
Thesis (Ph.D.)--University of Adelaide, Dept. of Animal Science, Waite Agricultural Research Institute, 1993
8

Hsu, ChingYi, and 許精益. "Analyzing the Active Site of Selenomonas ruminantium Phytase by Site-directed Mutagenesis and X-ray Crystallography." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/51404419758848221883.

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Abstract:
碩士
國立臺灣大學
生化科學研究所
92
Phytase can hydrolyzes phytate（myo-inositol hexaphosphate）during plant germination to produce phosphate（Pi）and inositol polyphasphate derivatives. In poultry and pig farms, phytase and phytate are fed to livestock as additives to provide Pi. In this study, we analyzed the active site of Selenomous ruminantium phytase . It exhibits higher catalytic activity than many other phytases. We wish our analysis could improve its applicability in the livestock industry. Most phytases can be classified into two big families: Histidine acid phytase family and Alkaline phytase family. S. ruminantium phytase, however, belongs to neither of them. Through structural alignment we have found that the active site of S. ruminantium phytase greatly resembles to members of the dual specificity phosphatase family in that it contains conserved Cys241 in the primary catalytic site, P-loop, and Asp212 and Pro216 in the auxiliary site, WPD-loop. To study the functions of these conserved amino acid residues, we employed site-directed mutagenesis to change Cys241 into Ser241 or Ala241, and Asp212 and Pro216 into Ala212 and Gly216, respectively, and measured their catalytic activity of these mutant forms. We found that the activity of P216G decreases as the temperatures increases, whereas mutations in Cys241 and Asp212 abrogate the activity of S. ruminantium phytase. These results suggest that these sites are very important for the function of S. ruminantium phytase. We also examined CD spectra of these mutant forms to test whether the increase in temperature causes conformational changes. To better understand the structural properties of phytase and its interaction with the substrates, C241A recombinant protein is over expressed in E. coli, and crystallized by using sodium malonate as precipitant, and subject to X-ray crystallography. We found that malonate binds into the active site of C214A. This observation has gain insight that how the competitive inhibition of polycarboxyl acid acts to the phytase active site.
9

Hsu, Ching-Yi, and 許精益. "Analyzing the Active Site of Selenomonas ruminantium Phytase by Site-directed Mutagenesis and X-ray Crystallography." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/56405004965771563781.

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Abstract:
碩士
國立臺灣大學
生化科學研究所
92
Phytase can hydrolyzes phytate（myo-inositol hexaphosphate）during plant germination to produce phosphate（Pi）and inositol polyphasphate derivatives. In poultry and pig farms, phytase and phytate are fed to livestock as additives to provide Pi. In this study, we analyzed the active site of Selenomous ruminantium phytase . It exhibits higher catalytic activity than many other phytases. We wish our analysis could improve its applicability in the livestock industry. Most phytases can be classified into two big families: Histidine acid phytase family and Alkaline phytase family. S. ruminantium phytase, however, belongs to neither of them. Through structural alignment we have found that the active site of S. ruminantium phytase greatly resembles to members of the dual specificity phosphatase family in that it contains conserved Cys241 in the primary catalytic site, P-loop, and Asp212 and Pro216 in the auxiliary site, WPD-loop. To study the functions of these conserved amino acid residues, we employed site-directed mutagenesis to change Cys241 into Ser241 or Ala241, and Asp212 and Pro216 into Ala212 and Gly216, respectively, and measured their catalytic activity of these mutant forms. We found that the activity of P216G decreases as the temperatures increases, whereas mutations in Cys241 and Asp212 abrogate the activity of S. ruminantium phytase. These results suggest that these sites are very important for the function of S. ruminantium phytase. We also examined CD spectra of these mutant forms to test whether the increase in temperature causes conformational changes. To better understand the structural properties of phytase and its interaction with the substrates, C241A recombinant protein is over expressed in E. coli, and crystallized by using sodium malonate as precipitant, and subject to X-ray crystallography. We found that malonate binds into the active site of C214A. This observation has gain insight that how the competitive inhibition of polycarboxyl acid acts to the phytase active site.

Book chapters on the topic "Selenomonas ruminantium":

1

Jordan, Douglas B., Xin-Liang Li, Christopher A. Dunlap, Terence R. Whitehead, and Michael A. Cotta. "β-d-Xylosidase From Selenomonas ruminantium of Glycoside Hydrolase Family 43." In Applied Biochemistry and Biotecnology, 93–104. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-181-3_9.

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2

Richardson, Anthony J., and Colin S. Stewart. "Hydrogen Transfer Between Neocallimastix Frontalis and Selenomonas Ruminantium Grown in Mixed Culture." In Microbiology and Biochemistry of Strict Anaerobes Involved in Interspecies Hydrogen Transfer, 463–65. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0613-9_60.

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3

Jordan, Douglas B. "B-d-Xylosidase from Selenomonas ruminantium: Catalyzed Reactions with Natural and Artificial Substrates." In Biotechnology for Fuels and Chemicals, 257–69. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-526-2_27.

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4

Aizawa, Shin-Ichi. "Selenomonas ruminantium — The Authentic Lateral Flagella." In The Flagellar World, 78–79. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-417234-0.00025-6.

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