메뉴 건너뛰기
Applied and Environmental Microbiology
Volumn 81, Issue 4, 2015, Pages 1338-1352
New mode of energy metabolism in the seventh order of methanogens as revealed by comparative genome analysis of "Candidatus Methanoplasma termitum"
Author keywords

[No Author keywords available]
Indexed keywords

GENES; HYDROGEN; METHANOGENS; PHYSIOLOGY;
EID: 84922051769     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03389-14     Document Type: Article
Times cited : (208)
References (87)
  • 1
    • 41349083576 scopus 로고    scopus 로고
    • Metabolic, phylogenetic, and ecological diversity of the methanogenic archaea
    • Liu Y, Whitman WB. 2008. Metabolic, phylogenetic, and ecological diversity of the methanogenic archaea. Ann N Y Acad Sci 1125:171-189. http://dx.doi.org/10.1196/annals.1419.019.
    • (2008) Ann N Y Acad Sci , vol.1125 , pp. 171-189
    • Liu, Y.1    Whitman, W.B.2
  • 2
    • 47549119041 scopus 로고    scopus 로고
    • Methanogenic archaea: ecologically relevant differences in energy conservation
    • Thauer RK, Kaster A-K, Seedorf H, Buckel W, Hedderich R. 2008. Methanogenic archaea: ecologically relevant differences in energy conservation. Nat Rev Microbiol 6:579-591. http://dx.doi.org/10.1038/nrmicro1931.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 579-591
    • Thauer, R.K.1    Kaster, A.-K.2    Seedorf, H.3    Buckel, W.4    Hedderich, R.5
  • 3
    • 20144364162 scopus 로고    scopus 로고
    • Higher-level classification of the Archaea: evolution of methanogenesis and methanogens
    • Bapteste E, Brochier C, Boucher Y. 2005. Higher-level classification of the Archaea: evolution of methanogenesis and methanogens. Archaea 1:353-363. http://dx.doi.org/10.1155/2005/859728.
    • (2005) Archaea , vol.1 , pp. 353-363
    • Bapteste, E.1    Brochier, C.2    Boucher, Y.3
  • 4
    • 84873138724 scopus 로고    scopus 로고
    • + bioenergetics in methanogenic archaea
    • + bioenergetics in methanogenic archaea. Biochem Soc Trans 41:421-426. http://dx.doi.org/10.1042/BST20120294.
    • (2013) Biochem Soc Trans , vol.41 , pp. 421-426
    • Schlegel, K.1    Müller, V.2
  • 5
    • 77954636353 scopus 로고    scopus 로고
    • Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase
    • Costa KC, Wong PM, Wang T, Lie TJ, Dodsworth JA, Swanson I, Burn JA, Hackett M, Leigh JA. 2010. Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase. Proc Natl Acad Sci U S A 107:11050-11055. http://dx.doi.org/10.1073/pnas.1003653107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11050-11055
    • Costa, K.C.1    Wong, P.M.2    Wang, T.3    Lie, T.J.4    Dodsworth, J.A.5    Swanson, I.6    Burn, J.A.7    Hackett, M.8    Leigh, J.A.9
  • 6
    • 79952588675 scopus 로고    scopus 로고
    • Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
    • Kaster A-K, Moll J, Parey K, Thauer RK. 2011. Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea. Proc Natl Acad Sci U S A 108:2981-2986. http://dx.doi.org/10.1073/pnas.1016761108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2981-2986
    • Kaster, A.-K.1    Moll, J.2    Parey, K.3    Thauer, R.K.4
  • 7
    • 0021763540 scopus 로고
    • Coupling of ATP synthesis and methane formation from methanol and molecular hydrogen in Methanosarcina barkeri
    • Blaut M, Gottschalk G. 1984. Coupling of ATP synthesis and methane formation from methanol and molecular hydrogen in Methanosarcina barkeri. Eur J Biochem 141:217-222. http://dx.doi.org/10.1111/j.1432-1033.1984.tb08178.x.
    • (1984) Eur J Biochem , vol.141 , pp. 217-222
    • Blaut, M.1    Gottschalk, G.2
  • 8
    • 0021921541 scopus 로고
    • Methanosphaera stadtmaniae gen. nov., sp. nov.: a species that forms methane by reducing methanol with hydrogen
    • Miller TL, Wolin MJ. 1985. Methanosphaera stadtmaniae gen. nov., sp. nov.: a species that forms methane by reducing methanol with hydrogen. Arch Microbiol 141:116-122. http://dx.doi.org/10.1007/BF00423270.
    • (1985) Arch Microbiol , vol.141 , pp. 116-122
    • Miller, T.L.1    Wolin, M.J.2
  • 9
    • 30744456055 scopus 로고    scopus 로고
    • The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis
    • Fricke WF, Seedorf H, Henne A, Kruer M, Liesegang H, Hedderich R, Gottschalk G, Thauer RK. 2006. The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis. J Bacteriol 188:642-658. http://dx.doi.org/10.1128/JB.188.2.642-658.2006.
    • (2006) J Bacteriol , vol.188 , pp. 642-658
    • Fricke, W.F.1    Seedorf, H.2    Henne, A.3    Kruer, M.4    Liesegang, H.5    Hedderich, R.6    Gottschalk, G.7    Thauer, R.K.8
  • 10
    • 0034519180 scopus 로고    scopus 로고
    • Methanomicrococcus blatticola gen. nov., sp. nov., a methanoland methylamine-reducing methanogen from the hindgut of the cockroach Periplaneta americana
    • Sprenger WW, van Belzen MC, Rosenberg J, Hackstein JHP, Keltjens JT. 2000. Methanomicrococcus blatticola gen. nov., sp. nov., a methanoland methylamine-reducing methanogen from the hindgut of the cockroach Periplaneta americana. Int J Syst Evol Microbiol 50:1989-1999. http://dx.doi.org/10.1099/00207713-50-6-1989.
    • (2000) Int J Syst Evol Microbiol , vol.50 , pp. 1989-1999
    • Sprenger, W.W.1    van Belzen, M.C.2    Rosenberg, J.3    Hackstein, J.H.P.4    Keltjens, J.T.5
  • 11
    • 25144465580 scopus 로고    scopus 로고
    • The energy metabolism of Methanomicrococcus blatticola: physiological and biochemical aspects
    • Sprenger WW, Hackstein JHP, Keltjens JT. 2005. The energy metabolism of Methanomicrococcus blatticola: physiological and biochemical aspects. Antonie Van Leeuwenhoek 87:289-299. http://dx.doi.org/10.1007/s10482-004-5941-5.
    • (2005) Antonie Van Leeuwenhoek , vol.87 , pp. 289-299
    • Sprenger, W.W.1    Hackstein, J.H.P.2    Keltjens, J.T.3
  • 12
    • 84870794077 scopus 로고    scopus 로고
    • "Methanoplasmatales," Thermoplasmatales-related archaea in termite guts and other environments, are the seventh order of methanogens
    • Paul K, Nonoh JO, Mikulski L, Brune A. 2012. "Methanoplasmatales," Thermoplasmatales-related archaea in termite guts and other environments, are the seventh order of methanogens. Appl Environ Microbiol 78:8245-8253. http://dx.doi.org/10.1128/AEM.02193-12.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 8245-8253
    • Paul, K.1    Nonoh, J.O.2    Mikulski, L.3    Brune, A.4
  • 13
    • 84864677092 scopus 로고    scopus 로고
    • Methanomassiliicoccus luminyensis gen. nov., sp. nov., a methanogenic archaeon isolated from human faeces
    • Dridi B, Fardeau M-L, Ollivier B, Raoult D, Drancourt M. 2012. Methanomassiliicoccus luminyensis gen. nov., sp. nov., a methanogenic archaeon isolated from human faeces. Int J Syst Evol Microbiol 62:1902-1907. http://dx.doi.org/10.1099/ijs.0.033712-0.
    • (2012) Int J Syst Evol Microbiol , vol.62 , pp. 1902-1907
    • Dridi, B.1    Fardeau, M.-L.2    Ollivier, B.3    Raoult, D.4    Drancourt, M.5
  • 14
    • 84890110026 scopus 로고    scopus 로고
    • Phylogenomic data support a seventh order of methylotrophic methanogens and provide insights into the evolution of methanogenesis
    • Borrel G, O'Toole PW, Harris HMB, Peyret P, Brugère J-F, Gribaldo S. 2013. Phylogenomic data support a seventh order of methylotrophic methanogens and provide insights into the evolution of methanogenesis. Genome Biol Evol 5:1769-1780. http://dx.doi.org/10.1093/gbe/evt128.
    • (2013) Genome Biol Evol , vol.5 , pp. 1769-1780
    • Borrel, G.1    O'Toole, P.W.2    Harris, H.M.B.3    Peyret, P.4    Brugère, J.-F.5    Gribaldo, S.6
  • 16
    • 84883808410 scopus 로고    scopus 로고
    • List of new names and new combinations previously effectively, but not validly, published
    • Oren A, Garrity GM. 2013. List of new names and new combinations previously effectively, but not validly, published. Int J Syst Evol Microbiol 63:3931-3934. http://dx.doi.org/10.1099/ijs.0.058222-0.
    • (2013) Int J Syst Evol Microbiol , vol.63 , pp. 3931-3934
    • Oren, A.1    Garrity, G.M.2
  • 17
    • 84870675165 scopus 로고    scopus 로고
    • Genome sequence of "Candidatus Methanomethylophilus alvus" Mx1201, a methanogenic archaeon from the human gut belonging to a seventh order of methanogens
    • Borrel G, Harris HMB, Tottey W, Mihajlosvki A, Parisot N, Peyretaillade E, Peyret P, Gribaldo S, O'Toole PW, Brugère J-F. 2012. Genome sequence of "Candidatus Methanomethylophilus alvus" Mx1201, a methanogenic archaeon from the human gut belonging to a seventh order of methanogens. J Bacteriol 194:6944-6945. http://dx.doi.org/10.1128/JB.01867-12.
    • (2012) J Bacteriol , vol.194 , pp. 6944-6945
    • Borrel, G.1    Harris, H.M.B.2    Tottey, W.3    Mihajlosvki, A.4    Parisot, N.5    Peyretaillade, E.6    Peyret, P.7    Gribaldo, S.8    O'Toole, P.W.9    Brugère, J.-F.10
  • 19
    • 84878500513 scopus 로고    scopus 로고
    • 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
    • Iino T, Tamaki H, Tamazawa S, Ueno Y, Ohkuma M, Suzuki K, Igarashi Y, Haruta S. 2013. 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 Environ 28:244-250. http://dx.doi.org/10.1264/jsme2.ME12189.
    • (2013) Microbes Environ , vol.28 , pp. 244-250
    • Iino, T.1    Tamaki, H.2    Tamazawa, S.3    Ueno, Y.4    Ohkuma, M.5    Suzuki, K.6    Igarashi, Y.7    Haruta, S.8
  • 20
    • 84866338044 scopus 로고    scopus 로고
    • Complete genome sequence of Methanomassiliicoccus luminyensis, the largest genome of a human-associated Archaea species
    • Gorlas A, Robert C, Gimenez G, Drancourt M, Raoult D. 2012. Complete genome sequence of Methanomassiliicoccus luminyensis, the largest genome of a human-associated Archaea species. J Bacteriol 194:4745. http://dx.doi.org/10.1128/JB.00956-12.
    • (2012) J Bacteriol , vol.194 , pp. 4745
    • Gorlas, A.1    Robert, C.2    Gimenez, G.3    Drancourt, M.4    Raoult, D.5
  • 21
    • 85052274144 scopus 로고    scopus 로고
    • Archaebiotics: proposed therapeutic use of archaea to prevent trimethylaminuria and cardiovascular disease
    • Brugère J-F, Borrel G, Gaci N, Tottey W, O'Toole PW, Malpuech-Brugère C. 2014. Archaebiotics: proposed therapeutic use of archaea to prevent trimethylaminuria and cardiovascular disease. Gut Microbes 5:5-10. http://dx.doi.org/10.4161/gmic.26749.
    • (2014) Gut Microbes , vol.5 , pp. 5-10
    • Brugère, J.-F.1    Borrel, G.2    Gaci, N.3    Tottey, W.4    O'Toole, P.W.5    Malpuech-Brugère, C.6
  • 23
    • 0037313265 scopus 로고    scopus 로고
    • Hydrogen-dependent oxygen reduction by homoacetogenic bacteria isolated from termite guts
    • Boga HI, Brune A. 2003. Hydrogen-dependent oxygen reduction by homoacetogenic bacteria isolated from termite guts. Appl Environ Microbiol 69:779-786. http://dx.doi.org/10.1128/AEM.69.2.779-786.2003.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 779-786
    • Boga, H.I.1    Brune, A.2
  • 24
    • 84855768808 scopus 로고    scopus 로고
    • Specificity of motor components in the dual flagellar system of Shewanella putrefaciens CN-32
    • Bubendorfer S, Held S, Windel N, Paulick A, Klingl A, Thormann KM. 2012. Specificity of motor components in the dual flagellar system of Shewanella putrefaciens CN-32. Mol Microbiol 83:335-350. http://dx.doi.org/10.1111/j.1365-2958.2011.07934.x.
    • (2012) Mol Microbiol , vol.83 , pp. 335-350
    • Bubendorfer, S.1    Held, S.2    Windel, N.3    Paulick, A.4    Klingl, A.5    Thormann, K.M.6
  • 25
    • 84879514835 scopus 로고    scopus 로고
    • Evidence for glycoprotein transport into complex plastids
    • Peschke M, Moog D, Klingl A, Maier UG, Hempel F. 2013. Evidence for glycoprotein transport into complex plastids. Proc Natl Acad Sci U S A 110:10860-10865. http://dx.doi.org/10.1073/pnas.1301945110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 10860-10865
    • Peschke, M.1    Moog, D.2    Klingl, A.3    Maier, U.G.4    Hempel, F.5
  • 28
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O. 2010. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol 59:307-321. http://dx.doi.org/10.1093/sysbio/syq010.
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 29
    • 29644441248 scopus 로고
    • Extraction of high molecular weightDNAfrom molluscs
    • Winnepenninckx B, Backeljau T, De Wachter R. 1993. Extraction of high molecular weightDNAfrom molluscs. Trends Genet 9:407. http://dx.doi.org/10.1016/0168-9525(93)90102-N.
    • (1993) Trends Genet , vol.9 , pp. 407
    • Winnepenninckx, B.1    Backeljau, T.2    De Wachter, R.3
  • 30
    • 84877090640 scopus 로고    scopus 로고
    • Poles apart: arctic and antarctic Octadecabacter strains share high genome plasticity and a new type of xanthorhodopsin
    • Vollmers J, Voget S, Dietrich S, Gollnow K, Smits M, Meyer K, Brinkhoff T, Simon M, Daniel R. 2013. Poles apart: arctic and antarctic Octadecabacter strains share high genome plasticity and a new type of xanthorhodopsin. PLoS One 8:e63422. http://dx.doi.org/10.1371/journal.pone.0063422.
    • (2013) PLoS One , vol.8
    • Vollmers, J.1    Voget, S.2    Dietrich, S.3    Gollnow, K.4    Smits, M.5    Meyer, K.6    Brinkhoff, T.7    Simon, M.8    Daniel, R.9
  • 31
    • 69949116874 scopus 로고    scopus 로고
    • IMG ER: a system for microbial genome annotation expert review and curation
    • Markowitz VM, Mavromatis K, Ivanova NN, Chen IA, Chu K, Kyrpides NC. 2009. IMG ER: a system for microbial genome annotation expert review and curation. Bioinformatics 25:2271-2278. http://dx.doi.org/10.1093/bioinformatics/btp393.
    • (2009) Bioinformatics , vol.25 , pp. 2271-2278
    • Markowitz, V.M.1    Mavromatis, K.2    Ivanova, N.N.3    Chen, I.A.4    Chu, K.5    Kyrpides, N.C.6
  • 34
    • 33846113652 scopus 로고    scopus 로고
    • TIGRFAMs and genome properties: tools for the assignment of molecular function and biological process in prokaryotic genomes
    • Selengut JD, Haft DH, Davidsen T, Ganapathy A, Gwinn-Giglio M, Nelson WC, Richter AR, White O. 2007. TIGRFAMs and genome properties: tools for the assignment of molecular function and biological process in prokaryotic genomes. Nucleic Acids Res 35:D260-D264. http://dx.doi.org/10.1093/nar/gkl1043.
    • (2007) Nucleic Acids Res , vol.35 , pp. D260-D264
    • Selengut, J.D.1    Haft, D.H.2    Davidsen, T.3    Ganapathy, A.4    Gwinn-Giglio, M.5    Nelson, W.C.6    Richter, A.R.7    White, O.8
  • 35
    • 75849158230 scopus 로고    scopus 로고
    • The Gene Ontology project in 2010: extensions and refinements
    • The Gene Ontology Consortium. 2010. The Gene Ontology project in 2010: extensions and refinements. Nucleic Acids Res 38:D331-D335. http://dx.doi.org/10.1093/nar/gkp1018.
    • (2010) Nucleic Acids Res , vol.38 , pp. D331-D335
  • 38
    • 84891760956 scopus 로고    scopus 로고
    • Data, information, knowledge and principle: back to metabolism in KEGG
    • Kanehisa M, Goto S, Sato Y, Kawashima M, Furumichi M, Tanabe M. 2014. Data, information, knowledge and principle: back to metabolism in KEGG. Nucleic Acids Res 42:D199-D205. http://dx.doi.org/10.1093/nar/gkt1076.
    • (2014) Nucleic Acids Res , vol.42 , pp. D199-D205
    • Kanehisa, M.1    Goto, S.2    Sato, Y.3    Kawashima, M.4    Furumichi, M.5    Tanabe, M.6
  • 40
    • 0020491364 scopus 로고
    • Organization of rRNA structural genes in the archaebacterium Thermoplasma acidophilum
    • Tu J, Zillig W. 1982. Organization of rRNA structural genes in the archaebacterium Thermoplasma acidophilum. Nucleic Acids Res 10:7231-7245. http://dx.doi.org/10.1093/nar/10.22.7231.
    • (1982) Nucleic Acids Res , vol.10 , pp. 7231-7245
    • Tu, J.1    Zillig, W.2
  • 41
    • 79953249251 scopus 로고    scopus 로고
    • The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine
    • Gaston MA, Zhang L, Green-Church KB, Krzycki JA. 2011. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471:647-650. http://dx.doi.org/10.1038/nature09918.
    • (2011) Nature , vol.471 , pp. 647-650
    • Gaston, M.A.1    Zhang, L.2    Green-Church, K.B.3    Krzycki, J.A.4
  • 42
    • 84896859974 scopus 로고    scopus 로고
    • Unique characteristics of the pyrrolysine system in the 7th order of methanogens: implications for the evolution of a genetic code expansion cassette
    • Borrel G, Gaci N, Peyret P, O'Toole PW, Gribaldo S, Brugère J-F. 2014. Unique characteristics of the pyrrolysine system in the 7th order of methanogens: implications for the evolution of a genetic code expansion cassette. Archaea 2014:374146. http://dx.doi.org/10.1155/2014/374146.
    • (2014) Archaea , vol.2014 , pp. 374146
    • Borrel, G.1    Gaci, N.2    Peyret, P.3    O'Toole, P.W.4    Gribaldo, S.5    Brugère, J.-F.6
  • 43
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: a tribute to Marjory Stephenson
    • Thauer RK. 1998. Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 144:2377-2406. http://dx.doi.org/10.1099/00221287-144-9-2377.
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 44
    • 0025877458 scopus 로고
    • Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin reductase, and heterodisulfide reductase in methanogenic bacteria
    • Schwörer B, Thauer R. 1991. Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin reductase, and heterodisulfide reductase in methanogenic bacteria. Arch Microbiol 155:459-465. http://dx.doi.org/10.1007/BF00244962.
    • (1991) Arch Microbiol , vol.155 , pp. 459-465
    • Schwörer, B.1    Thauer, R.2
  • 46
    • 0034005319 scopus 로고    scopus 로고
    • The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons
    • Paul L, Ferguson DJ, Krzycki J. 2000. The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons. J Bacteriol 182:2520-2529. http://dx.doi.org/10.1128/JB.182.9.2520-2529.2000.
    • (2000) J Bacteriol , vol.182 , pp. 2520-2529
    • Paul, L.1    Ferguson, D.J.2    Krzycki, J.3
  • 47
    • 0037165964 scopus 로고    scopus 로고
    • A new UAG-encoded residue in the structure of a methanogen methyltransferase
    • Hao B, Gong W, Ferguson TK, James CM, Krzycki JA, Chan MK. 2002. A new UAG-encoded residue in the structure of a methanogen methyltransferase. Science 296:1462-1466. http://dx.doi.org/10.1126/science.1069556.
    • (2002) Science , vol.296 , pp. 1462-1466
    • Hao, B.1    Gong, W.2    Ferguson, T.K.3    James, C.M.4    Krzycki, J.A.5    Chan, M.K.6
  • 48
    • 4644255236 scopus 로고    scopus 로고
    • Function of genetically encoded pyrrolysine in corrinoid- dependent methylamine methyltransferases
    • Krzycki JA. 2004. Function of genetically encoded pyrrolysine in corrinoid- dependent methylamine methyltransferases. Curr Opin Chem Biol 8:484-491. http://dx.doi.org/10.1016/j.cbpa.2004.08.012.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 484-491
    • Krzycki, J.A.1
  • 49
    • 0030946069 scopus 로고    scopus 로고
    • Reconstitution of monomethylamine: coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri
    • Burke SA, Krzycki JA. 1997. Reconstitution of monomethylamine: coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J Biol Chem 272: 16570-16577.
    • (1997) J Biol Chem , vol.272 , pp. 16570-16577
    • Burke, S.A.1    Krzycki, J.A.2
  • 50
    • 45749140542 scopus 로고    scopus 로고
    • Structure of the archaeal community of the rumen
    • Janssen PH, Kirs M. 2008. Structure of the archaeal community of the rumen. Appl Environ Microbiol 74:3619-3625. http://dx.doi.org/10.1128/AEM.02812-07.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 3619-3625
    • Janssen, P.H.1    Kirs, M.2
  • 52
    • 0033568398 scopus 로고    scopus 로고
    • Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases
    • Tersteegen A, Hedderich R. 1999. Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Eur J Biochem 264:930-943. http://dx.doi.org/10.1046/j.1432-1327.1999.00692.x.
    • (1999) Eur J Biochem , vol.264 , pp. 930-943
    • Tersteegen, A.1    Hedderich, R.2
  • 53
    • 84866550896 scopus 로고    scopus 로고
    • Essential anaplerotic role for the energy-converting hydrogenase Eha in hydrogenotrophic methanogenesis
    • Lie TJ, Costa KC, Lupa B, Korpole S, Whitman WB, Leigh JA. 2012. Essential anaplerotic role for the energy-converting hydrogenase Eha in hydrogenotrophic methanogenesis. Proc Natl Acad Sci U S A 109:15473-15478. http://dx.doi.org/10.1073/pnas.1208779109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 15473-15478
    • Lie, T.J.1    Costa, K.C.2    Lupa, B.3    Korpole, S.4    Whitman, W.B.5    Leigh, J.A.6
  • 54
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer J, Bartoschek S, Koch J, Künkel A, Hedderich R. 1999. Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur J Biochem 265:325-335. http://dx.doi.org/10.1046/j.1432-1327.1999.00738.x.
    • (1999) Eur J Biochem , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Künkel, A.4    Hedderich, R.5
  • 55
    • 77955246393 scopus 로고    scopus 로고
    • Involvement of Ech hydrogenase in energy conservation of Methanosarcina mazei
    • Welte C, Krätzer C, Deppenmeier U. 2010. Involvement of Ech hydrogenase in energy conservation of Methanosarcina mazei. FEBS J 277:3396-3403. http://dx.doi.org/10.1111/j.1742-4658.2010.07744.x.
    • (2010) FEBS J , vol.277 , pp. 3396-3403
    • Welte, C.1    Krätzer, C.2    Deppenmeier, U.3
  • 57
    • 84901851838 scopus 로고    scopus 로고
    • Bioenergetics and anaerobic respiratory chains of aceticlastic methanogens
    • Welte C, Deppenmeier U. 2014. Bioenergetics and anaerobic respiratory chains of aceticlastic methanogens. Biochim Biophys Acta 1837:1130-1147. http://dx.doi.org/10.1016/j.bbabio.2013.12.002.
    • (2014) Biochim Biophys Acta , vol.1837 , pp. 1130-1147
    • Welte, C.1    Deppenmeier, U.2
  • 58
    • 79961032041 scopus 로고    scopus 로고
    • The evolution of respiratory chain complex I from a smaller last common ancestor consisting of 11 protein subunits
    • Moparthi VK, Hägerhäll C. 2011. The evolution of respiratory chain complex I from a smaller last common ancestor consisting of 11 protein subunits. J Mol Evol 72:484-497. http://dx.doi.org/10.1007/s00239-011-9447-2.
    • (2011) J Mol Evol , vol.72 , pp. 484-497
    • Moparthi, V.K.1    Hägerhäll, C.2
  • 59
    • 79958142635 scopus 로고    scopus 로고
    • Membrane-bound electron transport in Methanosaeta thermophila
    • Welte C, Deppenmeier U. 2011. Membrane-bound electron transport in Methanosaeta thermophila. J Bacteriol 193:2868-2870. http://dx.doi.org/10.1128/JB.00162-11.
    • (2011) J Bacteriol , vol.193 , pp. 2868-2870
    • Welte, C.1    Deppenmeier, U.2
  • 60
    • 76449096786 scopus 로고    scopus 로고
    • Methanogenesis by Methanosarcina acetivorans involves two structurally and functionally distinct classes of heterodisulfide reductase
    • Buan NR, Metcalf WW. 2010. Methanogenesis by Methanosarcina acetivorans involves two structurally and functionally distinct classes of heterodisulfide reductase. Mol Microbiol 75:843-853. http://dx.doi.org/10.1111/j.1365-2958.2009.06990.x.
    • (2010) Mol Microbiol , vol.75 , pp. 843-853
    • Buan, N.R.1    Metcalf, W.W.2
  • 61
    • 84885365932 scopus 로고    scopus 로고
    • Functional role of the MrpA- and MrpDhomologous protein subunits in enzyme complexes evolutionary related to respiratory chain complex I
    • Moparthi VK, Kumar B, Al-Eryani Y, Sperling E, Görecki K, Drakenberg T, Hägerhäll C. 2014. Functional role of the MrpA- and MrpDhomologous protein subunits in enzyme complexes evolutionary related to respiratory chain complex I. Biochim Biophys Acta 1837:178-185. http://dx.doi.org/10.1016/j.bbabio.2013.09.012.
    • (2014) Biochim Biophys Acta , vol.1837 , pp. 178-185
    • Moparthi, V.K.1    Kumar, B.2    Al-Eryani, Y.3    Sperling, E.4    Görecki, K.5    Drakenberg, T.6    Hägerhäll, C.7
  • 62
    • 0037129849 scopus 로고    scopus 로고
    • Molecular characterization of phosphoglycerate mutase in archaea
    • van der Oost J, Huynen MA, Verhees CH. 2002. Molecular characterization of phosphoglycerate mutase in archaea. FEMS Microbiol Lett 212: 111-120. http://dx.doi.org/10.1111/j.1574-6968.2002.tb11253.x.
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 111-120
    • van der Oost, J.1    Huynen, M.A.2    Verhees, C.H.3
  • 63
    • 77951112274 scopus 로고    scopus 로고
    • Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme
    • Say RF, Fuchs G. 2010. Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral gluconeogenic enzyme. Nature 464:1077-1081. http://dx.doi.org/10.1038/nature08884.
    • (2010) Nature , vol.464 , pp. 1077-1081
    • Say, R.F.1    Fuchs, G.2
  • 64
    • 0019162521 scopus 로고
    • Nickel dependence of factor F430 content in Methanobacterium thermoautotrophicum
    • Diekert G, Weber B, Thauer RK. 1980. Nickel dependence of factor F430 content in Methanobacterium thermoautotrophicum. Arch Microbiol 127: 273-278. http://dx.doi.org/10.1007/BF00427204.
    • (1980) Arch Microbiol , vol.127 , pp. 273-278
    • Diekert, G.1    Weber, B.2    Thauer, R.K.3
  • 65
    • 0018873633 scopus 로고
    • Presence of nickel in factor F430 from Methanobacterium bryantii
    • Whitman WB, Wolfe RS. 1980. Presence of nickel in factor F430 from Methanobacterium bryantii. Biochem Biophys Res Commun 92:1196-1201. http://dx.doi.org/10.1016/0006-291X(80)90413-1.
    • (1980) Biochem Biophys Res Commun , vol.92 , pp. 1196-1201
    • Whitman, W.B.1    Wolfe, R.S.2
  • 66
    • 0028726343 scopus 로고
    • Biosynthesis of coenzyme F430, a nickel porphinoid involved in methanogenesis
    • Thauer RK, Bonacker LG. 1994. Biosynthesis of coenzyme F430, a nickel porphinoid involved in methanogenesis. Ciba Found Symp 180:210-222.
    • (1994) Ciba Found Symp , vol.180 , pp. 210-222
    • Thauer, R.K.1    Bonacker, L.G.2
  • 67
    • 84893707267 scopus 로고    scopus 로고
    • The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri
    • Kühner M, Haufschildt K, Neumann A, Storbeck S, Streif J, Layer G. 2014. The alternative route to heme in the methanogenic archaeon Methanosarcina barkeri. Archaea 2014:327637. http://dx.doi.org/10.1155/2014/327637.
    • (2014) Archaea , vol.2014 , pp. 327637
    • Kühner, M.1    Haufschildt, K.2    Neumann, A.3    Storbeck, S.4    Streif, J.5    Layer, G.6
  • 68
    • 0039196490 scopus 로고
    • Incorporation of methioninederived methyl groups into factor F430 by Methanobacterium thermoautotrophicum
    • Jaenchen R, Diekert G, Thauer RK. 1981. Incorporation of methioninederived methyl groups into factor F430 by Methanobacterium thermoautotrophicum. FEBS Lett 130:133-136. http://dx.doi.org/10.1016/0014-5793(81)80681-3.
    • (1981) FEBS Lett , vol.130 , pp. 133-136
    • Jaenchen, R.1    Diekert, G.2    Thauer, R.K.3
  • 69
    • 0037134521 scopus 로고    scopus 로고
    • Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonatebiosynthesizing enzymes
    • Graham DE, Xu H, White RH. 2002. Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonatebiosynthesizing enzymes. J Biol Chem 277:13421-13429. http://dx.doi.org/10.1074/jbc.M201011200.
    • (2002) J Biol Chem , vol.277 , pp. 13421-13429
    • Graham, D.E.1    Xu, H.2    White, R.H.3
  • 70
    • 73149115741 scopus 로고    scopus 로고
    • Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase
    • Graham DE, Taylor SM, Wolf RZ, Namboori SC. 2009. Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase. Biochem J 424: 467-478. http://dx.doi.org/10.1042/BJ20090999.
    • (2009) Biochem J , vol.424 , pp. 467-478
    • Graham, D.E.1    Taylor, S.M.2    Wolf, R.Z.3    Namboori, S.C.4
  • 71
    • 77249158769 scopus 로고    scopus 로고
    • Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: different role, different evolution
    • Ogawa T, Yoshimura T, Hemmi H. 2010. Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: different role, different evolution. Biochem Biophys Res Commun 393:16-20. http://dx.doi.org/10.1016/j.bbrc.2010.01.063.
    • (2010) Biochem Biophys Res Commun , vol.393 , pp. 16-20
    • Ogawa, T.1    Yoshimura, T.2    Hemmi, H.3
  • 72
    • 0028209988 scopus 로고
    • A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis
    • Tachibana A. 1994. A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis. FEBS Lett 341:291-294. http://dx.doi.org/10.1016/0014-5793(94)80475-3.
    • (1994) FEBS Lett , vol.341 , pp. 291-294
    • Tachibana, A.1
  • 73
    • 84901190009 scopus 로고    scopus 로고
    • A re-evaluation of the archaeal membrane lipid biosynthetic pathway
    • Villanueva L, Sinninghe Damsté JS, Schouten S. 2014. A re-evaluation of the archaeal membrane lipid biosynthetic pathway. Nat Rev Microbiol 12:438-448. http://dx.doi.org/10.1038/nrmicro3260.
    • (2014) Nat Rev Microbiol , vol.12 , pp. 438-448
    • Villanueva, L.1    Sinninghe Damsté, J.S.2    Schouten, S.3
  • 74
    • 84862754646 scopus 로고    scopus 로고
    • The archaellum: an old motility structure with a new name
    • Jarrell KF, Albers S-V. 2012. The archaellum: an old motility structure with a new name. Trends Microbiol 7:307-312. http://dx.doi.org/10.1016/j.tim.2012.04.007.
    • (2012) Trends Microbiol , vol.7 , pp. 307-312
    • Jarrell, K.F.1    Albers, S.-V.2
  • 75
    • 35148889967 scopus 로고    scopus 로고
    • Proteinaceous surface layers of Archaea: ultrastructure and biochemistry
    • In Cavicchioli R (ed), ASM Press, Washington, D.C.
    • König H, Rachel R, Claus H. 2007. Proteinaceous surface layers of Archaea: ultrastructure and biochemistry, p 315-340. In Cavicchioli R (ed), Archaea: molecular and cellular biology. ASM Press, Washington, D.C.
    • (2007) Archaea: molecular and cellular biology , pp. 315-340
    • König, H.1    Rachel, R.2    Claus, H.3
  • 77
    • 0012998399 scopus 로고    scopus 로고
    • The ultrastructure of Ignicoccus: evidence for a novel outer membrane and for intracellular vesicle budding in an archaeon
    • Rachel R, Wyschkony I, Riehl S, Huber H. 2002. The ultrastructure of Ignicoccus: evidence for a novel outer membrane and for intracellular vesicle budding in an archaeon. Archaea 1:9-18. http://dx.doi.org/10.1155/2002/307480.
    • (2002) Archaea , vol.1 , pp. 9-18
    • Rachel, R.1    Wyschkony, I.2    Riehl, S.3    Huber, H.4
  • 78
    • 58549108582 scopus 로고    scopus 로고
    • Three-dimensional analysis of the structure and ecology of a novel, ultrasmall archaeon
    • Comolli LR, Baker BJ, Downing KH, Siegerist CE, Banfield JF. 2009. Three-dimensional analysis of the structure and ecology of a novel, ultrasmall archaeon. ISME J 3:159-167. http://dx.doi.org/10.1038/ismej.2008.99.
    • (2009) ISME J , vol.3 , pp. 159-167
    • Comolli, L.R.1    Baker, B.J.2    Downing, K.H.3    Siegerist, C.E.4    Banfield, J.F.5
  • 79
    • 0017806024 scopus 로고
    • Chemical composition of the peptidoglycanfree cell wall of methanogenic bacteria
    • Kandler O, König H. 1978. Chemical composition of the peptidoglycanfree cell wall of methanogenic bacteria. Arch Microbiol 118:141-152. http://dx.doi.org/10.1007/BF00415722.
    • (1978) Arch Microbiol , vol.118 , pp. 141-152
    • Kandler, O.1    König, H.2
  • 80
    • 70349559191 scopus 로고    scopus 로고
    • Anaerobic oxidation of methane: progress with an unknown process
    • Knittel K, Boetius A. 2009. Anaerobic oxidation of methane: progress with an unknown process. Annu Rev Microbiol 63:311-334. http://dx.doi.org/10.1146/annurev.micro.61.080706.093130.
    • (2009) Annu Rev Microbiol , vol.63 , pp. 311-334
    • Knittel, K.1    Boetius, A.2
  • 81
    • 54849247900 scopus 로고    scopus 로고
    • Thermoplasmatales
    • In Dworkin M, Falkow S, Rosenberg E, Schleifer K-H, Stackebrandt E (ed),Springer, New York, N.Y.
    • Huber H, Stetter KO. 2006. Thermoplasmatales, p 101-112. In Dworkin M, Falkow S, Rosenberg E, Schleifer K-H, Stackebrandt E (ed), The prokaryotes, vol 3. Springer, New York, N.Y.
    • (2006) The prokaryotes , vol.3 , pp. 101-112
    • Huber, H.1    Stetter, K.O.2
  • 83
    • 84875889563 scopus 로고    scopus 로고
    • Microbial diversity in the deep-subsurface hydrothermal aquifer feeding the giant gypsum crystal-bearing Naica Mine, Mexico
    • Ragon M, Van Driessche AES, García-Ruíz JM, Moreira D, López-García P. 2013. Microbial diversity in the deep-subsurface hydrothermal aquifer feeding the giant gypsum crystal-bearing Naica Mine, Mexico. Front Microbiol 4:37. http://dx.doi.org/10.3389/fmicb.2013.00037.
    • (2013) Front Microbiol , vol.4 , pp. 37
    • Ragon, M.1    Van Driessche, A.E.S.2    García-Ruíz, J.M.3    Moreira, D.4    López-García, P.5
  • 85
    • 11144313963 scopus 로고
    • Thermoplasma acidophilum and Thermoplasma volcanium sp.nov. from solfatara fields
    • Segerer A, Langworthy TA, Stetter KO. 1988. Thermoplasma acidophilum and Thermoplasma volcanium sp. nov. from solfatara fields. Syst Appl Microbiol 10:161-171. http://dx.doi.org/10.1016/S0723-2020(88)80031-6.
    • (1988) Syst Appl Microbiol , vol.10 , pp. 161-171
    • Segerer, A.1    Langworthy, T.A.2    Stetter, K.O.3
  • 86
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer RK, Jungermann K, Decker K. 1977. Energy conservation in chemotrophic anaerobic bacteria. Bacteriol Rev 41:100-180.
    • (1977) Bacteriol Rev , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 87
    • 34247093387 scopus 로고    scopus 로고
    • The competitive success of Methanomicrococcus blatticola, a dominant methylotrophic methanogen in the cockroach hindgut, is supported by high substrate affinities and favorable thermodynamics
    • Sprenger WW, Hackstein JH, Keltjens JT. 2007. The competitive success of Methanomicrococcus blatticola, a dominant methylotrophic methanogen in the cockroach hindgut, is supported by high substrate affinities and favorable thermodynamics. FEMS Microbiol Ecol 60:266-275. http://dx.doi.org/10.1111/j.1574-6941.2007.00287.x.
    • (2007) FEMS Microbiol Ecol , vol.60 , pp. 266-275
    • Sprenger, W.W.1    Hackstein, J.H.2    Keltjens, J.T.3

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.