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Volume 2017 (2017), Article ID 2756573, 12 pages
https://doi.org/10.1155/2017/2756573
Research Article

Growth Characteristics of Methanomassiliicoccus luminyensis and Expression of Methyltransferase Encoding Genes

Institut für Mikrobiologie und Biotechnologie, Universität Bonn, Bonn, Germany

Correspondence should be addressed to Uwe Deppenmeier; ed.nnob-inu@neppedu

Received 18 July 2017; Accepted 24 September 2017; Published 2 November 2017

Academic Editor: William W. Metcalf

Copyright © 2017 Lena Kröninger et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. G. Ferry, “Fundamentals of methanogenic pathways that are key to the biomethanation of complex biomass,” Current Opinion in Biotechnology, vol. 22, no. 3, pp. 351–357, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. N. Gaci, G. Borrel, W. Tottey, P. W. O’Toole, and J. F. Brugère, “Archaea and the human gut: new beginning of an old story,” World Journal of Gastroenterology, vol. 20, no. 43, pp. 16062–16078, 2014. View at Publisher · View at Google Scholar · View at Scopus
  3. B. Dridi, M. L. Fardeau, B. Ollivier, D. Raoult, and M. Drancourt, “Methanomassiliicoccus luminyensis gen. nov., sp. nov., a methanogenic archaeon isolated from human faeces,” International Journal of Systematic and Evolutionary Microbiology, vol. 62, Part 8, pp. 1902–1907, 2012. View at Publisher · View at Google Scholar · View at Scopus
  4. K. Paul, J. O. Nonoh, L. Mikulski, and A. Brune, ““Methanoplasmatales,” Thermoplasmatales-related archaea in termite guts and other environments, are the seventh order of methanogens,” Applied and Environmental Microbiology, vol. 78, no. 23, pp. 8245–8253, 2012. View at Publisher · View at Google Scholar · View at Scopus
  5. G. Borrel, N. Parisot, H. M. Harris et al., “Comparative genomics highlights the unique biology of Methanomassiliicoccales, a Thermoplasmatales-related seventh order of methanogenic archaea that encodes pyrrolysine,” BMC Genomics, vol. 15, no. 1, pp. 679–701, 2014. View at Publisher · View at Google Scholar · View at Scopus
  6. T. Iino, H. Tamaki, S. Tamazawa et al., “Candidatus Methanogranum caenicola: a novel methanogen from the anaerobic digested sludge, and proposal of Methanomassiliicoccaceae fam. nov. and Methanomassiliicoccales ord. nov., for a methanogenic lineage of the class Thermoplasmata,” Microbes and Environments, vol. 28, no. 2, pp. 244–250, 2013. View at Publisher · View at Google Scholar · View at Scopus
  7. G. Borrel, P. W. O’Toole, H. M. Harris, P. Peyret, J. F. Brugère, and S. Gribaldo, “Phylogenomic data support a seventh order of methylotrophic methanogens and provide insights into the evolution of methanogenesis,” Genome Biology and Evolution, vol. 5, no. 10, pp. 1769–1780, 2013. View at Publisher · View at Google Scholar · View at Scopus
  8. U. Deppenmeier, “The unique biochemistry of methanogenesis,” Progress in Nucleic Acid Research and Molecular Biology, vol. 71, pp. 223–283, 2002. View at Publisher · View at Google Scholar
  9. T. L. Miller and M. J. Wolin, “Methanosphaera stadtmaniae gen. nov., sp. nov.: a species that forms methane by reducing methanol with hydrogen,” Archives of Microbiology, vol. 141, no. 2, pp. 116–122, 1985. View at Publisher · View at Google Scholar · View at Scopus
  10. W. F. Fricke, H. Seedorf, A. Henne et al., “The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis,” Journal of Bacteriology, vol. 188, no. 2, pp. 642–658, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. L. Kröninger, S. Berger, C. Welte, and U. Deppenmeier, “Evidence for the involvement of two different heterodisulfide reductases in the energy conserving system of Methanomassiliicoccus luminyensis,” FEBS Journal, vol. 283, no. 3, pp. 472–483, 2016. View at Publisher · View at Google Scholar · View at Scopus
  12. K. Lang, J. Schuldes, A. Klingl, A. Poehlein, R. Daniel, and A. Brune, “New mode of energy metabolism in the seventh order of methanogens as revealed by comparative genome analysis of “Candidatus Methanoplasma termitum”,” Applied and Environmental Microbiology, vol. 81, no. 4, pp. 1338–1352, 2015. View at Publisher · View at Google Scholar · View at Scopus
  13. G. Borrel, N. Gaci, P. Peyret, P. W. O’Toole, S. Gribaldo, and J. F. Brugère, “Unique characteristics of the pyrrolysine system in the 7th order of methanogens: implications for the evolution of a genetic code expansion cassette,” Archaea, vol. 2014, Article ID 374146, 11 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  14. J. F. Brugère, G. Borrel, N. Gaci, W. Tottey, P. W. O’Toole, and C. Malpuech-Brugère, “Archaebiotics: proposed therapeutic use of archaea to prevent trimethylaminuria and cardiovascular disease,” Gut Microbes, vol. 5, no. 1, pp. 5–10, 2014. View at Publisher · View at Google Scholar · View at Scopus
  15. R. J. Mackay, C. J. McEntyre, C. Henderson, M. Lever, and P. M. George, “Trimethylaminuria: causes and diagnosis of a socially distressing condition,” The Clinical Biochemist Review, vol. 32, no. 1, pp. 33-34, 2011. View at Google Scholar
  16. H. Hippe, D. Caspari, K. Fiebig, and G. Gottschalk, “Utilization of trimethylamine and other N-methyl compounds for growth and methane formation by Methanosarcina barkeri,” Proceedings of the National Academy of Sciences of the United States of America, vol. 76, no. 1, pp. 494–498, 1979. View at Publisher · View at Google Scholar
  17. C. Krätzer, P. Carini, R. Hovey, and U. Deppenmeier, “Transcriptional profiling of methyltransferase genes during growth of Methanosarcina mazei on trimethylamine,” Journal of Bacteriology, vol. 191, no. 16, pp. 5108–5115, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. M. A. Larkin, G. Blackshields, N. P. Brown et al., “Clustal W and Clustal X version 2.0,” Bioinformatics, vol. 23, no. 21, pp. 2947-2948, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. J. P. Folsom and R. P. Carlson, “Physiological, biomass elemental composition and proteomic analyses of Escherichia coli ammonium limited chemostat growth, and comparison with iron- and glucose-limited chemostat growth,” Microbiology, vol. 161, no. 8, pp. 1659–1670, 2015. View at Publisher · View at Google Scholar · View at Scopus
  20. L. Paul, D. J. Ferguson, and J. A. Krzycki, “The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons,” Journal of Bacteriology, vol. 182, no. 9, pp. 2520–2529, 2000. View at Publisher · View at Google Scholar · View at Scopus
  21. J. A. Krzycki, “The path of lysine to pyrrolysine,” Current Opinion in Chemical Biology, vol. 17, no. 4, pp. 619–625, 2013. View at Publisher · View at Google Scholar · View at Scopus
  22. K. Sauer, U. Harms, and R. K. Thauer, “Methanol: coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MT1,” European Journal of Biochemistry, vol. 243, no. 3, pp. 670–677, 1997. View at Publisher · View at Google Scholar
  23. R. K. Thauer, A. K. Kaster, H. Seedorf, W. Buckel, and R. Hedderich, “Methanogenic archaea: ecologically relevant differences in energy conservation,” Nature Reviews Microbiology, vol. 6, no. 8, pp. 579–591, 2008. View at Publisher · View at Google Scholar · View at Scopus
  24. A. K. Kaster, J. Moll, K. Parey, and R. K. Thauer, “Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 7, pp. 2981–2986, 2011. View at Publisher · View at Google Scholar · View at Scopus
  25. A. J. B. Zehnder and K. Wuhrmann, “Physiology of Methanobacterium strain AZ,” Archives of Microbiology, vol. 111, no. 3, pp. 199–205, 1977. View at Publisher · View at Google Scholar · View at Scopus
  26. A. M. Roberton and R. S. Wolfe, “Adenosine triphosphate pools in Methanobacterium,” Journal of Bacteriology, vol. 102, no. 1, pp. 43–51, 1970. View at Google Scholar
  27. J. A. Robinson and J. M. Tiedje, “Competition between sulfate-reducing and methanogenic bacteria for H2 under resting and growing conditions,” Archives of Microbiology, vol. 137, no. 1, pp. 26–32, 1984. View at Publisher · View at Google Scholar · View at Scopus
  28. P. J. Weimer and J. G. Zeikus, “One carbon metabolism in methanogenic bacteria,” Archives of Microbiology, vol. 119, no. 1, pp. 49–57, 1978. View at Publisher · View at Google Scholar · View at Scopus
  29. M. R. Smith and R. A. Mah, “Acetate as sole carbon and energy source for growth of Methanosarcina strain 227,” Applied and Environmental Microbiology, vol. 39, no. 5, pp. 993–999, 1980. View at Google Scholar
  30. M. R. Smith and R. A. Mah, “Growth and methanogenesis by Methanosarcina strain 227 on acetate and methanol,” Applied and Environmental Microbiology, vol. 36, no. 6, pp. 870–879, 1978. View at Google Scholar
  31. M. Rother and J. A. Krzycki, “Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea,” Archaea, vol. 2010, Article ID 453642, 14 pages, 2010. View at Publisher · View at Google Scholar · View at Scopus
  32. U. Harms and R. K. Thauer, “Methylcobalamin:coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli,” European Journal of Biochemistry, vol. 235, no. 3, pp. 653–659, 1996. View at Publisher · View at Google Scholar
  33. D. J. Ferguson Jr, J. A. Krzycki, and D. A. Grahame, “Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri,” Journal of Biological Chemistry, vol. 271, no. 9, pp. 5189–5194, 1996. View at Publisher · View at Google Scholar · View at Scopus
  34. D. J. Ferguson Jr and J. A. Krzycki, “Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri,” Journal of Bacteriology, vol. 179, no. 3, pp. 846–852, 1997. View at Publisher · View at Google Scholar
  35. S. A. Burke and J. A. Krzycki, “Reconstitution of monomethylamine:coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri,” Journal of Biological Chemistry, vol. 272, no. 26, pp. 16570–16577, 1997. View at Publisher · View at Google Scholar · View at Scopus
  36. D. J. Ferguson Jr, N. Gorlatova, D. A. Grahame, and J. A. Krzycki, “Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri,” Journal of Biological Chemistry, vol. 275, no. 37, pp. 29053–29060, 2000. View at Publisher · View at Google Scholar
  37. M. A. Pritchett and W. W. Metcalf, “Genetic, physiological and biochemical characterization of multiple methanol methyltransferase isozymes in Methanosarcina acetivorans C2A,” Molecular Microbiology, vol. 56, no. 5, pp. 1183–1194, 2005. View at Publisher · View at Google Scholar · View at Scopus
  38. S. A. Burke, S. L. Lo, and J. A. Krzycki, “Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine,” Journal of Bacteriology, vol. 180, no. 13, pp. 3432–3440, 1998. View at Google Scholar
  39. A. Bose, M. A. Pritchett, and W. W. Metcalf, “Genetic analysis of the methanol- and methylamine-specific methyltransferase 2 genes of Methanosarcina acetivorans C2A,” Journal of Bacteriology, vol. 190, no. 11, pp. 4017–4026, 2008. View at Publisher · View at Google Scholar · View at Scopus
  40. A. Bose, M. A. Pritchett, M. Rother, and W. W. Metcalf, “Differential regulation of the three methanol methyltransferase isozymes in Methanosarcina acetivorans C2A,” Journal of Bacteriology, vol. 188, no. 20, pp. 7274–7283, 2006. View at Publisher · View at Google Scholar · View at Scopus
  41. Y. H. Ding, S. P. Zhang, J. F. Tomb, and J. G. Ferry, “Genomic and proteomic analyses reveal multiple homologs of genes encoding enzymes of the methanol:coenzyme M methyltransferase system that are differentially expressed in methanol- and acetate-grown Methanosarcina thermophila,” FEMS Micrbiology Letters, vol. 215, no. 1, pp. 127–132, 2002. View at Publisher · View at Google Scholar · View at Scopus
  42. L. Li, Q. Li, L. Rohlin et al., “Quantitative proteomic and microarray analysis of the archaeon Methanosarcina acetivorans grown with acetate versus methanol,” Journal of Proteome Research, vol. 6, no. 2, pp. 759–771, 2007. View at Publisher · View at Google Scholar · View at Scopus
  43. A. Bose and W. W. Metcalf, “Distinct regulators control the expression of methanol methyltransferase isozymes in Methanosarcina acetivorans C2A,” Molecular Microbiology, vol. 67, no. 3, pp. 649–661, 2008. View at Publisher · View at Google Scholar · View at Scopus
  44. C. E. Garner, S. Smith, B. de Lacy Costello et al., “Volatile organic compounds from feces and their potential for diagnosis of gastrointestinal disease,” FASEB Journal, vol. 21, no. 8, pp. 1675–1688, 2007. View at Publisher · View at Google Scholar · View at Scopus