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Volumn 14, Issue 1, 2013, Pages

Comparative genomics in acid mine drainage biofilm communities reveals metabolic and structural differentiation of co-occurring archaea

Author keywords

Acid mine drainage; Comparative genomics; Ferroplasma; Iron oxidation; Metagenomics; Thermoplasmatales

Indexed keywords

COBALAMIN; HISTIDINE; LEUCINE; RNA 16S; VALINE;

EID: 84880182120     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-14-485     Document Type: Article
Times cited : (82)

References (119)
  • 2
    • 79952803560 scopus 로고    scopus 로고
    • Genome analyses of Icelandic strains of Sulfolobus islandicus, model organisms for genetic and virus-host interaction studies
    • 10.1128/JB.01487-10, 3067641, 21278296
    • Guo L, Brugger K, Liu C, Shah SA, Zheng HJ, Zhu YQ, Wang SY, Lillestol RK, Chen LM, Frank J, et al. Genome analyses of Icelandic strains of Sulfolobus islandicus, model organisms for genetic and virus-host interaction studies. J Bacteriol 2011, 193(7):1672-1680. 10.1128/JB.01487-10, 3067641, 21278296.
    • (2011) J Bacteriol , vol.193 , Issue.7 , pp. 1672-1680
    • Guo, L.1    Brugger, K.2    Liu, C.3    Shah, S.A.4    Zheng, H.J.5    Zhu, Y.Q.6    Wang, S.Y.7    Lillestol, R.K.8    Chen, L.M.9    Frank, J.10
  • 3
    • 66649087973 scopus 로고    scopus 로고
    • Biogeography of the Sulfolobus islandicus pan-genome
    • 10.1073/pnas.0808945106, 2689034, 19435847
    • Reno ML, Held NL, Fields CJ, Burke PV, Whitaker RJ. Biogeography of the Sulfolobus islandicus pan-genome. Proc Natl Acad Sci USA 2009, 106(21):8605-8610. 10.1073/pnas.0808945106, 2689034, 19435847.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.21 , pp. 8605-8610
    • Reno, M.L.1    Held, N.L.2    Fields, C.J.3    Burke, P.V.4    Whitaker, R.J.5
  • 4
    • 0042242559 scopus 로고    scopus 로고
    • Geographic barriers isolate endemic populations of hyperthermophilic archaea
    • 10.1126/science.1086909, 12881573
    • Whitaker RJ, Grogan DW, Taylor JW. Geographic barriers isolate endemic populations of hyperthermophilic archaea. Science 2003, 301(5635):976-978. 10.1126/science.1086909, 12881573.
    • (2003) Science , vol.301 , Issue.5635 , pp. 976-978
    • Whitaker, R.J.1    Grogan, D.W.2    Taylor, J.W.3
  • 5
    • 78149423315 scopus 로고    scopus 로고
    • Metagenomes from high-temperature chemotrophic systems reveal geochemical controls on microbial community structure and function
    • 10.1371/journal.pone.0009773, 2841643, 20333304
    • Inskeep WP, Rusch DB, Jay ZJ, Herrgard MJ, Kozubal MA, Richardson TH, Macur RE, Hamamura N, Jennings RD, Fouke BW, et al. Metagenomes from high-temperature chemotrophic systems reveal geochemical controls on microbial community structure and function. PLoS One 2010, 5(3):e9773. 10.1371/journal.pone.0009773, 2841643, 20333304.
    • (2010) PLoS One , vol.5 , Issue.3
    • Inskeep, W.P.1    Rusch, D.B.2    Jay, Z.J.3    Herrgard, M.J.4    Kozubal, M.A.5    Richardson, T.H.6    Macur, R.E.7    Hamamura, N.8    Jennings, R.D.9    Fouke, B.W.10
  • 7
    • 54849247900 scopus 로고    scopus 로고
    • From Thermoplasmatales
    • 233 Spring Street, New York, NY 10013, United States: Springer, Dworkin M, Falkow S, Rosenberg E, Schleifer KH, Stackebrandt E, 3
    • Huber H, Stetter KO. From Thermoplasmatales. Prokaryotes: A Handbook on the Biology of Bacteria, Vol 3 2006, 101-112. 233 Spring Street, New York, NY 10013, United States: Springer, Dworkin M, Falkow S, Rosenberg E, Schleifer KH, Stackebrandt E, 3.
    • (2006) Prokaryotes: A Handbook on the Biology of Bacteria, Vol 3 , pp. 101-112
    • Huber, H.1    Stetter, K.O.2
  • 8
    • 3242771843 scopus 로고    scopus 로고
    • Characterization of Ferroplasma isolates and Ferroplasma acidarmanus sp nov., extreme acidophiles from acid mine drainage and industrial bioleaching environments
    • 10.1128/AEM.70.4.2079-2088.2004, 383147, 15066799
    • Dopson M, Baker-Austin C, Hind A, Bowman JP, Bond PL. Characterization of Ferroplasma isolates and Ferroplasma acidarmanus sp nov., extreme acidophiles from acid mine drainage and industrial bioleaching environments. Appl Environ Microbiol 2004, 70(4):2079-2088. 10.1128/AEM.70.4.2079-2088.2004, 383147, 15066799.
    • (2004) Appl Environ Microbiol , vol.70 , Issue.4 , pp. 2079-2088
    • Dopson, M.1    Baker-Austin, C.2    Hind, A.3    Bowman, J.P.4    Bond, P.L.5
  • 9
    • 47249121250 scopus 로고    scopus 로고
    • Isolation and characterization of Ferroplasma thermophilum sp. nov., a novel extremely acidophilic, moderately thermophilic archaeon and its role in bioleaching of chalcopyrite
    • 10.1111/j.1365-2672.2008.03807.x, 18422958
    • Zhou H, Zhang R, Hu P, Zeng W, Xie Y, Wu C, Qiu G. Isolation and characterization of Ferroplasma thermophilum sp. nov., a novel extremely acidophilic, moderately thermophilic archaeon and its role in bioleaching of chalcopyrite. J Appl Microbiol 2008, 105(2):591-601. 10.1111/j.1365-2672.2008.03807.x, 18422958.
    • (2008) J Appl Microbiol , vol.105 , Issue.2 , pp. 591-601
    • Zhou, H.1    Zhang, R.2    Hu, P.3    Zeng, W.4    Xie, Y.5    Wu, C.6    Qiu, G.7
  • 10
    • 17144438252 scopus 로고    scopus 로고
    • Ferroplasma acidiphilum gen. nov., sp nov., an acidophilic, autotrophic, ferrous-iron-oxidizing, cell-wall-lacking, mesophilic member of the Ferroplasmaceae fam. nov., comprising a distinct lineage of the Archaea
    • 10.1099/00207713-50-3-997, 10843038
    • Golyshina OV, Pivovarova TA, Karavaiko GI, Kondrat'eva TF, Moore ERB, Abraham WR, Lunsdorf H, Timmis KN, Yakimov MM, Golyshin PN. Ferroplasma acidiphilum gen. nov., sp nov., an acidophilic, autotrophic, ferrous-iron-oxidizing, cell-wall-lacking, mesophilic member of the Ferroplasmaceae fam. nov., comprising a distinct lineage of the Archaea. Int J Syst Evol Microbiol 2000, 50:997-1006. 10.1099/00207713-50-3-997, 10843038.
    • (2000) Int J Syst Evol Microbiol , vol.50 , pp. 997-1006
    • Golyshina, O.V.1    Pivovarova, T.A.2    Karavaiko, G.I.3    Kondrat'eva, T.F.4    Moore, E.R.B.5    Abraham, W.R.6    Lunsdorf, H.7    Timmis, K.N.8    Yakimov, M.M.9    Golyshin, P.N.10
  • 11
    • 0034629254 scopus 로고    scopus 로고
    • An archaeal iron-oxidizing extreme acidophile important in acid mine drainage
    • 10.1126/science.287.5459.1796, 10710303
    • Edwards KJ, Bond PL, Gihring TM, Banfield JF. An archaeal iron-oxidizing extreme acidophile important in acid mine drainage. Science 2000, 287(5459):1796-1799. 10.1126/science.287.5459.1796, 10710303.
    • (2000) Science , vol.287 , Issue.5459 , pp. 1796-1799
    • Edwards, K.J.1    Bond, P.L.2    Gihring, T.M.3    Banfield, J.F.4
  • 12
    • 0014963118 scopus 로고
    • Thermophilic, acidophilic mycoplasma isolated from a coal refuse pile
    • 10.1126/science.170.3965.1416, 5481857
    • Darland G, Brock TD, Samsonof W, Conti SF. Thermophilic, acidophilic mycoplasma isolated from a coal refuse pile. Science 1970, 170(3965):1416-1418. 10.1126/science.170.3965.1416, 5481857.
    • (1970) Science , vol.170 , Issue.3965 , pp. 1416-1418
    • Darland, G.1    Brock, T.D.2    Samsonof, W.3    Conti, S.F.4
  • 13
    • 0029681421 scopus 로고    scopus 로고
    • Picrophilus oshimae and Picrophilus torridus fam nov, gen nov, sp nov, two species of hyperacidophilic, thermophilic, heterotrophic, aerobic archaea
    • Schleper C, Puhler G, Klenk HP, Zillig W. Picrophilus oshimae and Picrophilus torridus fam nov, gen nov, sp nov, two species of hyperacidophilic, thermophilic, heterotrophic, aerobic archaea. Int J Syst Bacteriol 1996, 46(3):814-816.
    • (1996) Int J Syst Bacteriol , vol.46 , Issue.3 , pp. 814-816
    • Schleper, C.1    Puhler, G.2    Klenk, H.P.3    Zillig, W.4
  • 14
    • 33751085608 scopus 로고    scopus 로고
    • Ferroplasma cupricumulans sp nov., a novel moderately thermophilic, acidophilic archaeon isolated from an industrial-scale chalcocite bioleach heap
    • 10.1007/s00792-006-0527-y, 16721487
    • Hawkes RB, Franzmann PD, O'Hara G, Plumb JJ. Ferroplasma cupricumulans sp nov., a novel moderately thermophilic, acidophilic archaeon isolated from an industrial-scale chalcocite bioleach heap. Extremophiles 2006, 10(6):525-530. 10.1007/s00792-006-0527-y, 16721487.
    • (2006) Extremophiles , vol.10 , Issue.6 , pp. 525-530
    • Hawkes, R.B.1    Franzmann, P.D.2    O'Hara, G.3    Plumb, J.J.4
  • 15
    • 36549000261 scopus 로고    scopus 로고
    • Thermogymnomonas acidicola gen. nov., sp nov., a novel thermoacidophilic, cell wall-less archaeon in the order Thermoplasmatales, isolated from a solfataric soil in Hakone, Japan
    • 10.1099/ijs.0.65203-0, 17978217
    • Itoh T, Yoshikawa N, Takashina T. Thermogymnomonas acidicola gen. nov., sp nov., a novel thermoacidophilic, cell wall-less archaeon in the order Thermoplasmatales, isolated from a solfataric soil in Hakone, Japan. Int J Syst Evol Microbiol 2007, 57:2557-2561. 10.1099/ijs.0.65203-0, 17978217.
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 2557-2561
    • Itoh, T.1    Yoshikawa, N.2    Takashina, T.3
  • 16
    • 80055092787 scopus 로고    scopus 로고
    • A semi-quantitative, synteny-based method to improve functional predictions for hypothetical and poorly annotated bacterial and archaeal genes
    • Yelton AP, Thomas BC, Simmons SL, Wilmes P, Zemla A, Thelen MP, Justice N, Banfield JF. A semi-quantitative, synteny-based method to improve functional predictions for hypothetical and poorly annotated bacterial and archaeal genes. PLoS Comp Biol 2011, 7(10):e1002230.
    • (2011) PLoS Comp Biol , vol.7 , Issue.10
    • Yelton, A.P.1    Thomas, B.C.2    Simmons, S.L.3    Wilmes, P.4    Zemla, A.5    Thelen, M.P.6    Justice, N.7    Banfield, J.F.8
  • 18
    • 84355162257 scopus 로고    scopus 로고
    • Community genomic analysis of an extremely acidophilic sulfur-oxidizing biofilm
    • 10.1038/ismej.2011.75, 3246232, 21716305
    • Jones DS, Albrecht HL, Dawson KS, Schaperdoth I, Freeman KH, Pi YD, Pearson A, Macalady JL. Community genomic analysis of an extremely acidophilic sulfur-oxidizing biofilm. ISME J 2012, 6(1):158-170. 10.1038/ismej.2011.75, 3246232, 21716305.
    • (2012) ISME J , vol.6 , Issue.1 , pp. 158-170
    • Jones, D.S.1    Albrecht, H.L.2    Dawson, K.S.3    Schaperdoth, I.4    Freeman, K.H.5    Pi, Y.D.6    Pearson, A.7    Macalady, J.L.8
  • 19
    • 84867649459 scopus 로고    scopus 로고
    • Archaea in organic-lean and organic-rich marine subsurface sediments: an environmental gradient reflected in distinct phylogenetic lineages
    • 3364523, 22666218
    • Durbin AM, Teske A. Archaea in organic-lean and organic-rich marine subsurface sediments: an environmental gradient reflected in distinct phylogenetic lineages. Front Microbiol 2012, 3:168. 3364523, 22666218.
    • (2012) Front Microbiol , vol.3 , pp. 168
    • Durbin, A.M.1    Teske, A.2
  • 21
    • 79955006053 scopus 로고    scopus 로고
    • Archaeal diversity in a terrestrial acidic spring field revealed by a novel PCR primer targeting archaeal 16S rRNA genes
    • 10.1111/j.1574-6968.2011.02267.x, 21410512
    • Kato S, Itoh T, Yamagishi A. Archaeal diversity in a terrestrial acidic spring field revealed by a novel PCR primer targeting archaeal 16S rRNA genes. FEMS Microbiol Lett 2011, 319(1):34-43. 10.1111/j.1574-6968.2011.02267.x, 21410512.
    • (2011) FEMS Microbiol Lett , vol.319 , Issue.1 , pp. 34-43
    • Kato, S.1    Itoh, T.2    Yamagishi, A.3
  • 22
    • 71449100076 scopus 로고    scopus 로고
    • Mapping the tree of life: Progress and prospects
    • 10.1128/MMBR.00033-09, 2786576, 19946133
    • Pace NR. Mapping the tree of life: Progress and prospects. Microbiol Mol Biol Rev 2009, 73(4):565-576. 10.1128/MMBR.00033-09, 2786576, 19946133.
    • (2009) Microbiol Mol Biol Rev , vol.73 , Issue.4 , pp. 565-576
    • Pace, N.R.1
  • 23
    • 35048898799 scopus 로고    scopus 로고
    • Genetic exchange across a species boundary in the archaeal genus Ferroplasma
    • 10.1534/genetics.107.072892, 2013692, 17603112
    • Eppley JM, Tyson GW, Getz WM, Banfield JF. Genetic exchange across a species boundary in the archaeal genus Ferroplasma. Genetics 2007, 177(1):407-416. 10.1534/genetics.107.072892, 2013692, 17603112.
    • (2007) Genetics , vol.177 , Issue.1 , pp. 407-416
    • Eppley, J.M.1    Tyson, G.W.2    Getz, W.M.3    Banfield, J.F.4
  • 24
    • 24944587193 scopus 로고    scopus 로고
    • Towards a genome-based taxonomy for prokaryotes
    • 10.1128/JB.187.18.6258-6264.2005, 1236649, 16159757
    • Konstantinidis KT, Tiedje JM. Towards a genome-based taxonomy for prokaryotes. J Bacteriol 2005, 187(18):6258-6264. 10.1128/JB.187.18.6258-6264.2005, 1236649, 16159757.
    • (2005) J Bacteriol , vol.187 , Issue.18 , pp. 6258-6264
    • Konstantinidis, K.T.1    Tiedje, J.M.2
  • 25
    • 33847280283 scopus 로고    scopus 로고
    • Prediction of effective genome size in metagenomic samples
    • 10.1186/gb-2007-8-1-r10, 1839125, 17224063
    • Raes J, Korbel JO, Lercher MJ, von Mering C, Bork P. Prediction of effective genome size in metagenomic samples. Genome Biol 2007, 8(1):R10. 10.1186/gb-2007-8-1-r10, 1839125, 17224063.
    • (2007) Genome Biol , vol.8 , Issue.1
    • Raes, J.1    Korbel, J.O.2    Lercher, M.J.3    von Mering, C.4    Bork, P.5
  • 27
    • 0036773132 scopus 로고    scopus 로고
    • Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8
    • 10.1016/S0969-2126(02)00855-9, 12377127
    • Niwa H, Tsuchiya D, Makyio H, Yoshida M, Morikawa K. Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure 2002, 10(10):1415-1423. 10.1016/S0969-2126(02)00855-9, 12377127.
    • (2002) Structure , vol.10 , Issue.10 , pp. 1415-1423
    • Niwa, H.1    Tsuchiya, D.2    Makyio, H.3    Yoshida, M.4    Morikawa, K.5
  • 29
    • 44349192011 scopus 로고    scopus 로고
    • Electron microscopy encounters with unusual thermophiles helps direct genomic analysis of Aciduliprofundum boonei
    • 10.1111/j.1472-4669.2008.00152.x, 18445019
    • Reysenbach AL, Flores GE. Electron microscopy encounters with unusual thermophiles helps direct genomic analysis of Aciduliprofundum boonei. Geobiology 2008, 6(3):331-336. 10.1111/j.1472-4669.2008.00152.x, 18445019.
    • (2008) Geobiology , vol.6 , Issue.3 , pp. 331-336
    • Reysenbach, A.L.1    Flores, G.E.2
  • 30
    • 36248931035 scopus 로고    scopus 로고
    • Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer
    • 10.1016/j.jmb.2007.10.042, 17996897
    • Abu-Qarn M, Yurist-Doutsch S, Giordano A, Trauner A, Morris HR, Hitchen P, Medalia O, Dell A, Eichler J. Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. J Mol Biol 2007, 374(5):1224-1236. 10.1016/j.jmb.2007.10.042, 17996897.
    • (2007) J Mol Biol , vol.374 , Issue.5 , pp. 1224-1236
    • Abu-Qarn, M.1    Yurist-Doutsch, S.2    Giordano, A.3    Trauner, A.4    Morris, H.R.5    Hitchen, P.6    Medalia, O.7    Dell, A.8    Eichler, J.9
  • 31
    • 0029566235 scopus 로고
    • Glycan structure of a heptose-containing S-layer glycoprotein of Bacillus thermoaerophilus
    • 10.1093/glycob/5.8.791, 8720077
    • Kosma P, Wugeditsch T, Christian R, Zayni S, Messner P. Glycan structure of a heptose-containing S-layer glycoprotein of Bacillus thermoaerophilus. Glycobiology 1995, 5(8):791-796. 10.1093/glycob/5.8.791, 8720077.
    • (1995) Glycobiology , vol.5 , Issue.8 , pp. 791-796
    • Kosma, P.1    Wugeditsch, T.2    Christian, R.3    Zayni, S.4    Messner, P.5
  • 32
    • 0032766054 scopus 로고    scopus 로고
    • Structural heterogeneity in the core oligosaccharide of the S-layer glycoprotein from Aneurinibacillus thermoaerophilus DSM 10155
    • 10.1093/glycob/9.8.787, 10406844
    • Wugeditsch T, Zachara NE, Puchberger M, Kosma P, Gooley AA, Messner P. Structural heterogeneity in the core oligosaccharide of the S-layer glycoprotein from Aneurinibacillus thermoaerophilus DSM 10155. Glycobiology 1999, 9(8):787-795. 10.1093/glycob/9.8.787, 10406844.
    • (1999) Glycobiology , vol.9 , Issue.8 , pp. 787-795
    • Wugeditsch, T.1    Zachara, N.E.2    Puchberger, M.3    Kosma, P.4    Gooley, A.A.5    Messner, P.6
  • 33
    • 0036066728 scopus 로고    scopus 로고
    • Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides
    • Valvano MA, Messner P, Kosma P. Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology-Sgm 2002, 148:1979-1989.
    • (2002) Microbiology-Sgm , vol.148 , pp. 1979-1989
    • Valvano, M.A.1    Messner, P.2    Kosma, P.3
  • 34
    • 0141741231 scopus 로고    scopus 로고
    • The microbiology of acidic mine waters
    • 10.1016/S0923-2508(03)00114-1, 14499932
    • Johnson DB, Hallberg KB. The microbiology of acidic mine waters. Res Microbiol 2003, 154(7):466-473. 10.1016/S0923-2508(03)00114-1, 14499932.
    • (2003) Res Microbiol , vol.154 , Issue.7 , pp. 466-473
    • Johnson, D.B.1    Hallberg, K.B.2
  • 35
    • 0033015720 scopus 로고    scopus 로고
    • Mechanism of pyrite dissolution in the presence of Thiobacillus ferrooxidans
    • 91446, 10388693
    • Fowler TA, Holmes PR, Crundwell FK. Mechanism of pyrite dissolution in the presence of Thiobacillus ferrooxidans. Appl Environ Microbiol 1999, 65(7):2987-2993. 91446, 10388693.
    • (1999) Appl Environ Microbiol , vol.65 , Issue.7 , pp. 2987-2993
    • Fowler, T.A.1    Holmes, P.R.2    Crundwell, F.K.3
  • 36
    • 26844536951 scopus 로고    scopus 로고
    • From characteristics and adaptability of iron- and sulfur-oxidizing microorganisms used for the recovery of metals from minerals and their concentrates
    • 10.1186/1475-2859-4-1, 544838, 15629064
    • Rawlings DE. From characteristics and adaptability of iron- and sulfur-oxidizing microorganisms used for the recovery of metals from minerals and their concentrates. Microb Cell Fact 2005, 4:1. 10.1186/1475-2859-4-1, 544838, 15629064.
    • (2005) Microb Cell Fact , vol.4 , pp. 1
    • Rawlings, D.E.1
  • 37
    • 0016813825 scopus 로고
    • Respiratory chain of Thiobacillus ferrooxidans: Reduction of cytochromes by Fe2+ and preliminary characterization of rusticyanin, a novel blue copper protein
    • 10.1016/0014-5793(75)80411-X, 6319
    • Cobley JG, Haddock BA. Respiratory chain of Thiobacillus ferrooxidans: Reduction of cytochromes by Fe2+ and preliminary characterization of rusticyanin, a novel blue copper protein. FEBS Lett 1975, 60(1):29-33. 10.1016/0014-5793(75)80411-X, 6319.
    • (1975) FEBS Lett , vol.60 , Issue.1 , pp. 29-33
    • Cobley, J.G.1    Haddock, B.A.2
  • 38
    • 0032697794 scopus 로고    scopus 로고
    • Interaction-induced redox switch in the electron transfer complex rusticyanin-cytochrome c(4)
    • 10.1074/jbc.274.43.30365, 10521412
    • Giudici-Orticoni MT, Guerlesquin F, Bruschi M, Nitschke W. Interaction-induced redox switch in the electron transfer complex rusticyanin-cytochrome c(4). J Biol Chem 1999, 274(43):30365-30369. 10.1074/jbc.274.43.30365, 10521412.
    • (1999) J Biol Chem , vol.274 , Issue.43 , pp. 30365-30369
    • Giudici-Orticoni, M.T.1    Guerlesquin, F.2    Bruschi, M.3    Nitschke, W.4
  • 39
    • 54449094393 scopus 로고    scopus 로고
    • A new iron-oxidizing/O-2-reducing supercomplex spanning both inner and outer membranes, isolated from the extreme acidophile Acidithiobacillus ferrooxidans
    • 10.1074/jbc.M802496200, 3258861, 18632666
    • Castelle C, Guiral M, Malarte G, Ledgham F, Leroy G, Brugna M, Giudici-Orticoni M-T. A new iron-oxidizing/O-2-reducing supercomplex spanning both inner and outer membranes, isolated from the extreme acidophile Acidithiobacillus ferrooxidans. J Biol Chem 2008, 283(38):25803-25811. 10.1074/jbc.M802496200, 3258861, 18632666.
    • (2008) J Biol Chem , vol.283 , Issue.38 , pp. 25803-25811
    • Castelle, C.1    Guiral, M.2    Malarte, G.3    Ledgham, F.4    Leroy, G.5    Brugna, M.6    Giudici-Orticoni, M.-T.7
  • 40
    • 0034691286 scopus 로고    scopus 로고
    • Characterization of a new dihemic c(4)-type cytochrome isolated from Thiobacillus ferrooxidans
    • Giudici-Orticoni MT, Leroy G, Nitschke W, Bruschi M. Characterization of a new dihemic c(4)-type cytochrome isolated from Thiobacillus ferrooxidans. Biochemistry (Mosc) 2000, 39(24):7205-7211.
    • (2000) Biochemistry (Mosc) , vol.39 , Issue.24 , pp. 7205-7211
    • Giudici-Orticoni, M.T.1    Leroy, G.2    Nitschke, W.3    Bruschi, M.4
  • 41
    • 17844394680 scopus 로고    scopus 로고
    • Insight into molecular stability and physiological properties of the diheme cytochrome CYC41 from the acidophilic bacterium Acidithiobacillus ferrooxidans
    • Malarte G, Leroy G, Lojou E, Abergel C, Bruschi M, Giudici-Orticoni MT. Insight into molecular stability and physiological properties of the diheme cytochrome CYC41 from the acidophilic bacterium Acidithiobacillus ferrooxidans. Biochemistry (Mosc) 2005, 44(17):6471-6481.
    • (2005) Biochemistry (Mosc) , vol.44 , Issue.17 , pp. 6471-6481
    • Malarte, G.1    Leroy, G.2    Lojou, E.3    Abergel, C.4    Bruschi, M.5    Giudici-Orticoni, M.T.6
  • 42
    • 4344634473 scopus 로고    scopus 로고
    • Regulation of the expression of the Acidithiobacillus ferrooxidans rus operon encoding two cytochromes c, a cytochrome oxidase and rusticyanin
    • 10.1099/mic.0.26966-0, 15256554
    • Yarzabal A, Appia-Ayme C, Ratouchniak J, Bonnefoy V. Regulation of the expression of the Acidithiobacillus ferrooxidans rus operon encoding two cytochromes c, a cytochrome oxidase and rusticyanin. Microbiology 2004, 150:2113-2123. 10.1099/mic.0.26966-0, 15256554.
    • (2004) Microbiology , vol.150 , pp. 2113-2123
    • Yarzabal, A.1    Appia-Ayme, C.2    Ratouchniak, J.3    Bonnefoy, V.4
  • 43
    • 4143137531 scopus 로고    scopus 로고
    • Differential protein expression during growth of Acidithiobacillus ferrooxidans on ferrous iron, sulfur compounds, or metal sulfides
    • 10.1128/AEM.70.8.4491-4498.2004, 492426, 15294777
    • Ramirez P, Guiliani N, Valenzuela L, Beard S, Jerez CA. Differential protein expression during growth of Acidithiobacillus ferrooxidans on ferrous iron, sulfur compounds, or metal sulfides. Appl Environ Microbiol 2004, 70(8):4491-4498. 10.1128/AEM.70.8.4491-4498.2004, 492426, 15294777.
    • (2004) Appl Environ Microbiol , vol.70 , Issue.8 , pp. 4491-4498
    • Ramirez, P.1    Guiliani, N.2    Valenzuela, L.3    Beard, S.4    Jerez, C.A.5
  • 46
    • 33747750273 scopus 로고    scopus 로고
    • Proteomic and bioinformatic analysis of iron- and sulfur-oxidizing Acidithiobacillus ferrooxidans using immobilized pH gradients and mass spectrometry
    • 10.1002/pmic.200500719, 16807941
    • Bouchal P, Zdrahal Z, Helanova S, Janiczek O, Hallberg KB, Mandl M. Proteomic and bioinformatic analysis of iron- and sulfur-oxidizing Acidithiobacillus ferrooxidans using immobilized pH gradients and mass spectrometry. Proteomics 2006, 6(15):4278-4285. 10.1002/pmic.200500719, 16807941.
    • (2006) Proteomics , vol.6 , Issue.15 , pp. 4278-4285
    • Bouchal, P.1    Zdrahal, Z.2    Helanova, S.3    Janiczek, O.4    Hallberg, K.B.5    Mandl, M.6
  • 47
    • 50249093201 scopus 로고    scopus 로고
    • The rus operon genes are differentially regulated when Acidithiobacillus ferrooxidans LR is kept in contact with metal sulfides
    • 10.1007/s00284-008-9208-7, 18665419
    • Carlos C, Reis FC, Vicentini R, Madureira DJ, Ottoboni LMM. The rus operon genes are differentially regulated when Acidithiobacillus ferrooxidans LR is kept in contact with metal sulfides. Curr Microbiol 2008, 57(4):375-380. 10.1007/s00284-008-9208-7, 18665419.
    • (2008) Curr Microbiol , vol.57 , Issue.4 , pp. 375-380
    • Carlos, C.1    Reis, F.C.2    Vicentini, R.3    Madureira, D.J.4    Ottoboni, L.M.M.5
  • 48
    • 84920081702 scopus 로고    scopus 로고
    • Genetic and bioinformatic insights into iron and sulfur oxidation mechanisms of bioleaching organisms
    • Berlin Heidelberg: Springer-Verlag, Rawlings DE, Johnson DB
    • Holmes DS, Bonnefoy V. Genetic and bioinformatic insights into iron and sulfur oxidation mechanisms of bioleaching organisms. Biomining 2007, 281-307. Berlin Heidelberg: Springer-Verlag, Rawlings DE, Johnson DB.
    • (2007) Biomining , pp. 281-307
    • Holmes, D.S.1    Bonnefoy, V.2
  • 50
    • 29244458671 scopus 로고    scopus 로고
    • Analysis of differential protein expression during growth states of Ferroplasma strains and insights into electron transport for iron oxidation
    • 10.1099/mic.0.28362-0, 16339958
    • Dopson M, Baker-Austin C, Bond PL. Analysis of differential protein expression during growth states of Ferroplasma strains and insights into electron transport for iron oxidation. Microbiology 2005, 151:4127-4137. 10.1099/mic.0.28362-0, 16339958.
    • (2005) Microbiology , vol.151 , pp. 4127-4137
    • Dopson, M.1    Baker-Austin, C.2    Bond, P.L.3
  • 51
    • 0033259961 scopus 로고    scopus 로고
    • Blue copper proteins as honorary cytochromes: The structure and evolution of blue copper proteins
    • Ambler RP. Blue copper proteins as honorary cytochromes: The structure and evolution of blue copper proteins. J Chem Soc Pak 1999, 21(3):213-228.
    • (1999) J Chem Soc Pak , vol.21 , Issue.3 , pp. 213-228
    • Ambler, R.P.1
  • 52
    • 0028207017 scopus 로고
    • Plastocyanin: Structural and functional analysis
    • 10.1007/BF00763219, 8027022
    • Redinbo MR, Yeates TO, Merchant S. Plastocyanin: Structural and functional analysis. J Bioenerg Biomembr 1994, 26(1):49-66. 10.1007/BF00763219, 8027022.
    • (1994) J Bioenerg Biomembr , vol.26 , Issue.1 , pp. 49-66
    • Redinbo, M.R.1    Yeates, T.O.2    Merchant, S.3
  • 53
    • 2942589291 scopus 로고    scopus 로고
    • The linked conservation of structure and function in a family of high diversity: The monomeric cupredoxins
    • 10.1016/j.str.2004.03.029, 15274913
    • Gough J, Chothia C. The linked conservation of structure and function in a family of high diversity: The monomeric cupredoxins. Structure 2004, 12(6):917-925. 10.1016/j.str.2004.03.029, 15274913.
    • (2004) Structure , vol.12 , Issue.6 , pp. 917-925
    • Gough, J.1    Chothia, C.2
  • 54
    • 13244279481 scopus 로고    scopus 로고
    • Functionally specified protein signatures distinctive for each of the different blue copper proteins
    • Giri AV, Anishetty S, Gautam P. Functionally specified protein signatures distinctive for each of the different blue copper proteins. BMC Bioinforma 2004, 5:127.
    • (2004) BMC Bioinforma , vol.5 , pp. 127
    • Giri, A.V.1    Anishetty, S.2    Gautam, P.3
  • 56
    • 0035808241 scopus 로고    scopus 로고
    • Sulfocyanin and subunit II, two copper proteins with novel features, provide new insight into the archaeal SoxM oxidase supercomplex
    • 10.1016/S0014-5793(00)02343-7, 11163357
    • Komorowski L, Schafer G. Sulfocyanin and subunit II, two copper proteins with novel features, provide new insight into the archaeal SoxM oxidase supercomplex. FEBS Lett 2001, 487(3):351-355. 10.1016/S0014-5793(00)02343-7, 11163357.
    • (2001) FEBS Lett , vol.487 , Issue.3 , pp. 351-355
    • Komorowski, L.1    Schafer, G.2
  • 57
    • 0036868094 scopus 로고    scopus 로고
    • The archaeal respiratory supercomplex SoxM from S. acidocaldarius combines features of quinole and cytochrome c oxidases
    • Komorowski L, Verheyen W, Schaefer G. The archaeal respiratory supercomplex SoxM from S. acidocaldarius combines features of quinole and cytochrome c oxidases. Biol Chem 2002, 383(11):1791-1799.
    • (2002) Biol Chem , vol.383 , Issue.11 , pp. 1791-1799
    • Komorowski, L.1    Verheyen, W.2    Schaefer, G.3
  • 58
    • 0033546326 scopus 로고    scopus 로고
    • Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes I. Characterization of the cytochrome bc(1)-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans
    • 10.1074/jbc.274.24.16760, 10358017
    • Elbehti A, Nitschke W, Tron P, Michel C, Lemesle-Meunier D. Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes I. Characterization of the cytochrome bc(1)-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans. J Biol Chem 1999, 274(24):16760-16765. 10.1074/jbc.274.24.16760, 10358017.
    • (1999) J Biol Chem , vol.274 , Issue.24 , pp. 16760-16765
    • Elbehti, A.1    Nitschke, W.2    Tron, P.3    Michel, C.4    Lemesle-Meunier, D.5
  • 59
    • 0032755413 scopus 로고    scopus 로고
    • Characterization of an operon encoding two c-type cytochromes, an aa(3)-type cytochrome oxidase, and rusticyanin in Thiobacillus ferrooxidans ATCC 33020
    • 91644, 10543786
    • Appia-Ayme C, Guiliani N, Ratouchniak J, Bonnefoy V. Characterization of an operon encoding two c-type cytochromes, an aa(3)-type cytochrome oxidase, and rusticyanin in Thiobacillus ferrooxidans ATCC 33020. Appl Environ Microbiol 1999, 65(11):4781-4787. 91644, 10543786.
    • (1999) Appl Environ Microbiol , vol.65 , Issue.11 , pp. 4781-4787
    • Appia-Ayme, C.1    Guiliani, N.2    Ratouchniak, J.3    Bonnefoy, V.4
  • 60
    • 17944400111 scopus 로고    scopus 로고
    • Rusticyanin gene expression of Acidithiobacillus ferrooxidans ATCC 33020 in sulfur- and in ferrous iron media
    • Yarzabal A, Duquesne K, Bonnefoy V. Rusticyanin gene expression of Acidithiobacillus ferrooxidans ATCC 33020 in sulfur- and in ferrous iron media. Hydrometallurgy 2003, 71(1-2):107-114.
    • (2003) Hydrometallurgy , vol.71 , Issue.1-2 , pp. 107-114
    • Yarzabal, A.1    Duquesne, K.2    Bonnefoy, V.3
  • 61
    • 2142693754 scopus 로고    scopus 로고
    • Molecular and culture-based analyses of aerobic carbon monoxide oxidizer diversity
    • 10.1128/AEM.69.12.7257-7265.2003, 309980, 14660374
    • King GA. Molecular and culture-based analyses of aerobic carbon monoxide oxidizer diversity. Appl Environ Microbiol 2003, 69(12):7257-7265. 10.1128/AEM.69.12.7257-7265.2003, 309980, 14660374.
    • (2003) Appl Environ Microbiol , vol.69 , Issue.12 , pp. 7257-7265
    • King, G.A.1
  • 62
    • 79953029156 scopus 로고    scopus 로고
    • Correlating carbon monoxide oxidation with cox genes in the abundant marine Roseobacter clade
    • 10.1038/ismej.2010.170, 3105738, 21068776
    • Cunliffe M. Correlating carbon monoxide oxidation with cox genes in the abundant marine Roseobacter clade. ISME J 2011, 5(4):685-691. 10.1038/ismej.2010.170, 3105738, 21068776.
    • (2011) ISME J , vol.5 , Issue.4 , pp. 685-691
    • Cunliffe, M.1
  • 64
    • 33846143212 scopus 로고    scopus 로고
    • Towards determining details of anaerobic growth coupled to ferric iron reduction by the acidophilic archaeon 'Ferroplasma acidarmanus' Fer1
    • 10.1007/s00792-006-0029-y, 17048042
    • Dopson M, Baker-Austin C, Bond P. Towards determining details of anaerobic growth coupled to ferric iron reduction by the acidophilic archaeon 'Ferroplasma acidarmanus' Fer1. Extremophiles 2007, 11(1):159-168. 10.1007/s00792-006-0029-y, 17048042.
    • (2007) Extremophiles , vol.11 , Issue.1 , pp. 159-168
    • Dopson, M.1    Baker-Austin, C.2    Bond, P.3
  • 66
    • 11144313963 scopus 로고
    • Thermoplasma acidophilum and Thermoplasma volcanium sp nov from solfatara fields
    • Segerer A, Langworthy TA, Stetter KO. Thermoplasma acidophilum and Thermoplasma volcanium sp nov from solfatara fields. Syst Appl Microbiol 1988, 10(2):161-171.
    • (1988) Syst Appl Microbiol , vol.10 , Issue.2 , pp. 161-171
    • Segerer, A.1    Langworthy, T.A.2    Stetter, K.O.3
  • 68
    • 0642312313 scopus 로고    scopus 로고
    • Evolution of mosaic operons by horizontal gene transfer and gene displacement in situ
    • 10.1186/gb-2003-4-9-r55, 193655, 12952534
    • Omelchenko MV, Makarova KS, Wolf YI, Rogozin IB, Koonin EV. Evolution of mosaic operons by horizontal gene transfer and gene displacement in situ. Genome Biol 2003, 4(9):R55. 10.1186/gb-2003-4-9-r55, 193655, 12952534.
    • (2003) Genome Biol , vol.4 , Issue.9
    • Omelchenko, M.V.1    Makarova, K.S.2    Wolf, Y.I.3    Rogozin, I.B.4    Koonin, E.V.5
  • 69
    • 0037122944 scopus 로고    scopus 로고
    • Quinol : fumarate oxidoreductases and succinate : quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment
    • Lemos RS, Fernandes AS, Pereira MM, Gomes CM, Teixeira M. Quinol : fumarate oxidoreductases and succinate : quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment. Biochim Biophys Acta 2002, 1553(1-2):158-170.
    • (2002) Biochim Biophys Acta , vol.1553 , Issue.1-2 , pp. 158-170
    • Lemos, R.S.1    Fernandes, A.S.2    Pereira, M.M.3    Gomes, C.M.4    Teixeira, M.5
  • 72
  • 73
    • 79955973710 scopus 로고    scopus 로고
    • Micron-scale Fe(2+)/Fe(3+), intermediate sulfur species and O(2) gradients across the biofilm-solution-sediment interface control biofilm organization
    • Ma S, Banfield JF. Micron-scale Fe(2+)/Fe(3+), intermediate sulfur species and O(2) gradients across the biofilm-solution-sediment interface control biofilm organization. Geochim Cosmochim Acta 2011, 75(12):3568-3580.
    • (2011) Geochim Cosmochim Acta , vol.75 , Issue.12 , pp. 3568-3580
    • Ma, S.1    Banfield, J.F.2
  • 74
    • 0025973280 scopus 로고
    • Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite
    • 207294, 1704886
    • Huang CJ, Barrett EL. Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite. J Bacteriol 1991, 173(4):1544-1553. 207294, 1704886.
    • (1991) J Bacteriol , vol.173 , Issue.4 , pp. 1544-1553
    • Huang, C.J.1    Barrett, E.L.2
  • 75
    • 33644607016 scopus 로고    scopus 로고
    • Identification of proteins present in the archaeon Thermoplasma volcanium cultured in aerobic or anaerobic conditions
    • Kawashima T, Yokoyama K, Higuchi S, Suzuki M. Identification of proteins present in the archaeon Thermoplasma volcanium cultured in aerobic or anaerobic conditions. Proc Jpn Acad Ser B Phys Biol Sci 2005, 81(6):204-219.
    • (2005) Proc Jpn Acad Ser B Phys Biol Sci , vol.81 , Issue.6 , pp. 204-219
    • Kawashima, T.1    Yokoyama, K.2    Higuchi, S.3    Suzuki, M.4
  • 76
    • 77956320089 scopus 로고    scopus 로고
    • Quantitative proteome and transcriptome analysis of the archaeon Thermoplasma acidophilum cultured under aerobic and anaerobic conditions
    • 10.1021/pr100567u, 20669988
    • Sun N, Pan CP, Nickell S, Mann M, Baumeister W, Nagy I. Quantitative proteome and transcriptome analysis of the archaeon Thermoplasma acidophilum cultured under aerobic and anaerobic conditions. J Proteome Res 2010, 9(9):4839-4850. 10.1021/pr100567u, 20669988.
    • (2010) J Proteome Res , vol.9 , Issue.9 , pp. 4839-4850
    • Sun, N.1    Pan, C.P.2    Nickell, S.3    Mann, M.4    Baumeister, W.5    Nagy, I.6
  • 78
    • 32444448426 scopus 로고    scopus 로고
    • Glyceraldehyde dehydrogenases from the thermoacidophilic euryarchaeota Picrophilus torridus and Thermoplasma acidophilum, key enzymes of the non-phosphorylative Entner-Doudoroff pathway, constitute a novel enzyme family within the aldehyde dehydrogenase superfamily
    • 10.1016/j.febslet.2006.01.029, 16458304
    • Reher M, Schonheit P. Glyceraldehyde dehydrogenases from the thermoacidophilic euryarchaeota Picrophilus torridus and Thermoplasma acidophilum, key enzymes of the non-phosphorylative Entner-Doudoroff pathway, constitute a novel enzyme family within the aldehyde dehydrogenase superfamily. FEBS Lett 2006, 580(5):1198-1204. 10.1016/j.febslet.2006.01.029, 16458304.
    • (2006) FEBS Lett , vol.580 , Issue.5 , pp. 1198-1204
    • Reher, M.1    Schonheit, P.2
  • 79
    • 0022549877 scopus 로고
    • Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaebacterium Thermoplasma acidophilum
    • Budgen N, Danson MJ. Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaebacterium Thermoplasma acidophilum. FEBS Lett 1986, 196(2):207-210.
    • (1986) FEBS Lett , vol.196 , Issue.2 , pp. 207-210
    • Budgen, N.1    Danson, M.J.2
  • 80
    • 0021696802 scopus 로고
    • Glucose-metabolism in the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus
    • 1144446, 6440533
    • Derosa M, Gambacorta A, Nicolaus B, Giardina P, Poerio E, Buonocore V. Glucose-metabolism in the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus. Biochem J 1984, 224(2):407-414. 1144446, 6440533.
    • (1984) Biochem J , vol.224 , Issue.2 , pp. 407-414
    • Derosa, M.1    Gambacorta, A.2    Nicolaus, B.3    Giardina, P.4    Poerio, E.5    Buonocore, V.6
  • 81
    • 12144290887 scopus 로고    scopus 로고
    • Reconstruction of the central carbohydrate metabolism of Thermoproteus tenax by use of genomic and biochemical data
    • 10.1128/JB.186.7.2179-2194.2004, 374391, 15028704
    • Siebers B, Tjaden B, Michalke K, Dorr C, Ahmed H, Zaparty M, Gordon P, Sensen CW, Zibat A, Klenk HP, et al. Reconstruction of the central carbohydrate metabolism of Thermoproteus tenax by use of genomic and biochemical data. J Bacteriol 2004, 186(7):2179-2194. 10.1128/JB.186.7.2179-2194.2004, 374391, 15028704.
    • (2004) J Bacteriol , vol.186 , Issue.7 , pp. 2179-2194
    • Siebers, B.1    Tjaden, B.2    Michalke, K.3    Dorr, C.4    Ahmed, H.5    Zaparty, M.6    Gordon, P.7    Sensen, C.W.8    Zibat, A.9    Klenk, H.P.10
  • 82
    • 75749149349 scopus 로고    scopus 로고
    • The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate-specific aldolase
    • 10.1128/JB.01281-09, 2812977, 20023024
    • Reher M, Fuhrer T, Bott M, Schoenheit P. The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate-specific aldolase. J Bacteriol 2010, 192(4):964-974. 10.1128/JB.01281-09, 2812977, 20023024.
    • (2010) J Bacteriol , vol.192 , Issue.4 , pp. 964-974
    • Reher, M.1    Fuhrer, T.2    Bott, M.3    Schoenheit, P.4
  • 83
    • 68449092955 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases: Dynamic history of protein family evolution
    • 10.1007/s00239-009-9263-0, 19639238
    • Swigonova Z, Mohsen AW, Vockley J. Acyl-CoA dehydrogenases: Dynamic history of protein family evolution. J Mol Evol 2009, 69(2):176-193. 10.1007/s00239-009-9263-0, 19639238.
    • (2009) J Mol Evol , vol.69 , Issue.2 , pp. 176-193
    • Swigonova, Z.1    Mohsen, A.W.2    Vockley, J.3
  • 84
    • 45749109478 scopus 로고    scopus 로고
    • Microbial communities in contaminated sediments, associated with bioremediation of uranium to submicromolar levels
    • 10.1128/AEM.02308-07, 2446554, 18456853
    • Cardenas E, Wu W, Leigh M, Carley J, Carroll S, Gentry T, Luo J, Watson D, Gu B, Ginder-Vogel M. Microbial communities in contaminated sediments, associated with bioremediation of uranium to submicromolar levels. Appl Environ Microbiol 2008, 74:3718-3729. 10.1128/AEM.02308-07, 2446554, 18456853.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 3718-3729
    • Cardenas, E.1    Wu, W.2    Leigh, M.3    Carley, J.4    Carroll, S.5    Gentry, T.6    Luo, J.7    Watson, D.8    Gu, B.9    Ginder-Vogel, M.10
  • 86
    • 35748958389 scopus 로고    scopus 로고
    • Production of methanethiol and volatile sulfur compounds by the archaeon " Ferroplasma acidarmanus"
    • 10.1007/s00792-007-0108-8, 17914603
    • Baumler DJ, Hung KF, Jeong KC, Kaspar CW. Production of methanethiol and volatile sulfur compounds by the archaeon " Ferroplasma acidarmanus" Extremophiles 2007, 11(6):841-851. 10.1007/s00792-007-0108-8, 17914603.
    • (2007) Extremophiles , vol.11 , Issue.6 , pp. 841-851
    • Baumler, D.J.1    Hung, K.F.2    Jeong, K.C.3    Kaspar, C.W.4
  • 87
    • 58549114486 scopus 로고    scopus 로고
    • Natural acidophilic biofilm communities reflect distinct organismal and functional organization
    • 10.1038/ismej.2008.90, 18843299
    • Wilmes P, Remis JP, Hwang M, Auer M, Thelen MP, Banfield JF. Natural acidophilic biofilm communities reflect distinct organismal and functional organization. ISME J 2009, 3(2):266-270. 10.1038/ismej.2008.90, 18843299.
    • (2009) ISME J , vol.3 , Issue.2 , pp. 266-270
    • Wilmes, P.1    Remis, J.P.2    Hwang, M.3    Auer, M.4    Thelen, M.P.5    Banfield, J.F.6
  • 88
    • 0027329154 scopus 로고
    • Acetyl-Coa synthetase (ADP forming) in archaea, a novel enzyme involved in acetate formation and ATP synthesis
    • Schafer T, Selig M, Schonheit P. Acetyl-Coa synthetase (ADP forming) in archaea, a novel enzyme involved in acetate formation and ATP synthesis. Arch Microbiol 1993, 159(1):72-83.
    • (1993) Arch Microbiol , vol.159 , Issue.1 , pp. 72-83
    • Schafer, T.1    Selig, M.2    Schonheit, P.3
  • 89
    • 6344253194 scopus 로고    scopus 로고
    • Unusual ADP-forming acetyl-coenzyme A synthetases from the mesophilic halophilic euryarchaeon Haloarcula marismortui and from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum
    • 10.1007/s00203-004-0702-4, 15340786
    • Brasen C, Schonheit P. Unusual ADP-forming acetyl-coenzyme A synthetases from the mesophilic halophilic euryarchaeon Haloarcula marismortui and from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Arch Microbiol 2004, 182(4):277-287. 10.1007/s00203-004-0702-4, 15340786.
    • (2004) Arch Microbiol , vol.182 , Issue.4 , pp. 277-287
    • Brasen, C.1    Schonheit, P.2
  • 90
    • 0036082038 scopus 로고    scopus 로고
    • Novel energy metabolism in anaerobic hyperthermophilic archaea: A modified Embden-Meyerhof pathway
    • Sakuraba H, Ohshima T. Novel energy metabolism in anaerobic hyperthermophilic archaea: A modified Embden-Meyerhof pathway. J Biosci Bioeng 2002, 93(5):441-448.
    • (2002) J Biosci Bioeng , vol.93 , Issue.5 , pp. 441-448
    • Sakuraba, H.1    Ohshima, T.2
  • 91
    • 27844507018 scopus 로고    scopus 로고
    • Unusual pathways and enzymes of central carbohydrate metabolism in Archaea
    • 10.1016/j.mib.2005.10.014, 16256419
    • Siebers B, Schonheit P. Unusual pathways and enzymes of central carbohydrate metabolism in Archaea. Curr Opin Microbiol 2005, 8(6):695-705. 10.1016/j.mib.2005.10.014, 16256419.
    • (2005) Curr Opin Microbiol , vol.8 , Issue.6 , pp. 695-705
    • Siebers, B.1    Schonheit, P.2
  • 92
    • 8844232661 scopus 로고    scopus 로고
    • Regulation of acetate and acetyl-CoA converting enzymes during growth on acetate and/or glucose in the halophilic archaeon Haloarcula marismortui
    • 10.1016/j.femsle.2004.09.033, 15556705
    • Brasen C, Schonheit P. Regulation of acetate and acetyl-CoA converting enzymes during growth on acetate and/or glucose in the halophilic archaeon Haloarcula marismortui. FEMS Microbiol Lett 2004, 241(1):21-26. 10.1016/j.femsle.2004.09.033, 15556705.
    • (2004) FEMS Microbiol Lett , vol.241 , Issue.1 , pp. 21-26
    • Brasen, C.1    Schonheit, P.2
  • 94
    • 77956803428 scopus 로고    scopus 로고
    • Identification of a novel class of membrane-bound NiFe-hydrogenases in Thermococcus onnurineus NA1 by in silico analysis
    • 10.1128/AEM.00123-10, 2937479, 20656864
    • Lim JK, Kang SG, Lebedinsky AV, Lee JH, Lee HS. Identification of a novel class of membrane-bound NiFe-hydrogenases in Thermococcus onnurineus NA1 by in silico analysis. Appl Environ Microbiol 2010, 76(18):6286-6289. 10.1128/AEM.00123-10, 2937479, 20656864.
    • (2010) Appl Environ Microbiol , vol.76 , Issue.18 , pp. 6286-6289
    • Lim, J.K.1    Kang, S.G.2    Lebedinsky, A.V.3    Lee, J.H.4    Lee, H.S.5
  • 95
    • 0027167618 scopus 로고
    • Microbial hydrogenases: Primary structure, classification, signatures and phylogeny
    • Wu LF, Mandrand MA. Microbial hydrogenases: Primary structure, classification, signatures and phylogeny. FEMS Microbiol Rev 1993, 104(3-4):243-270.
    • (1993) FEMS Microbiol Rev , vol.104 , Issue.3-4 , pp. 243-270
    • Wu, L.F.1    Mandrand, M.A.2
  • 96
    • 84887411953 scopus 로고    scopus 로고
    • Microbial populations and distribution at an extreme acid mine drainage environment: A study using fluorescent in-situ hybridization [abstract]
    • Edwards KJ, Gihring TM, Schrenk MO, Hamers RJ, Banfield JF. Microbial populations and distribution at an extreme acid mine drainage environment: A study using fluorescent in-situ hybridization [abstract]. Abstr Gen Meet Am Soc Microbiol 1998, 98:382.
    • (1998) Abstr Gen Meet Am Soc Microbiol , vol.98 , pp. 382
    • Edwards, K.J.1    Gihring, T.M.2    Schrenk, M.O.3    Hamers, R.J.4    Banfield, J.F.5
  • 97
    • 0042102003 scopus 로고    scopus 로고
    • Arsenic resistance in the archaeon " Ferroplasma acidarmanus" : new insights into the structure and evolution of the ars genes
    • Gihring TM, Bond PL, Peters SC, Banfield JF. Arsenic resistance in the archaeon " Ferroplasma acidarmanus" : new insights into the structure and evolution of the ars genes. Extremophiles 2003, 7(2):123-130.
    • (2003) Extremophiles , vol.7 , Issue.2 , pp. 123-130
    • Gihring, T.M.1    Bond, P.L.2    Peters, S.C.3    Banfield, J.F.4
  • 98
    • 23844471958 scopus 로고    scopus 로고
    • Molecular insight into extreme copper resistance in the extremophilic archaeon 'Ferroplasma acidarmanus' Fer1
    • 10.1099/mic.0.28076-0, 16079342
    • Baker-Austin C, Dopson M, Wexler M, Sawers RG, Bond PL. Molecular insight into extreme copper resistance in the extremophilic archaeon 'Ferroplasma acidarmanus' Fer1. Microbiology 2005, 151:2637-2646. 10.1099/mic.0.28076-0, 16079342.
    • (2005) Microbiology , vol.151 , pp. 2637-2646
    • Baker-Austin, C.1    Dopson, M.2    Wexler, M.3    Sawers, R.G.4    Bond, P.L.5
  • 99
    • 84982623266 scopus 로고
    • Molecular mechanisms of copper resistance and accumulation in bacteria
    • 10.1111/j.1574-6976.1994.tb00112.x, 7917425
    • Cooksey DA. Molecular mechanisms of copper resistance and accumulation in bacteria. FEMS Microbiol Rev 1994, 14(4):381-386. 10.1111/j.1574-6976.1994.tb00112.x, 7917425.
    • (1994) FEMS Microbiol Rev , vol.14 , Issue.4 , pp. 381-386
    • Cooksey, D.A.1
  • 101
    • 0029881205 scopus 로고    scopus 로고
    • Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae
    • 10.1046/j.1365-2958.1996.5371058.x, 8736544
    • Jarrell KF, Bayley DP, Florian V, Klein A. Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae. Mol Microbiol 1996, 20(3):657-666. 10.1046/j.1365-2958.1996.5371058.x, 8736544.
    • (1996) Mol Microbiol , vol.20 , Issue.3 , pp. 657-666
    • Jarrell, K.F.1    Bayley, D.P.2    Florian, V.3    Klein, A.4
  • 102
    • 0036436988 scopus 로고    scopus 로고
    • Mutants in flaI and flaJ of the archaeon Methanococcus voltae are deficient in flagellum assembly
    • 10.1046/j.1365-2958.2002.03220.x, 12410843
    • Thomas NA, Mueller S, Klein A, Jarrell KF. Mutants in flaI and flaJ of the archaeon Methanococcus voltae are deficient in flagellum assembly. Mol Microbiol 2002, 46(3):879-887. 10.1046/j.1365-2958.2002.03220.x, 12410843.
    • (2002) Mol Microbiol , vol.46 , Issue.3 , pp. 879-887
    • Thomas, N.A.1    Mueller, S.2    Klein, A.3    Jarrell, K.F.4
  • 103
    • 0034888193 scopus 로고    scopus 로고
    • Insertional inactivation of the flaH gene in the archaeon Methanococcus voltae results in non-flagellated cells
    • 10.1007/s004380100451, 11459179
    • Thomas NA, Pawson CT, Jarrell KF. Insertional inactivation of the flaH gene in the archaeon Methanococcus voltae results in non-flagellated cells. Mol Genet Genomics 2001, 265(4):596-603. 10.1007/s004380100451, 11459179.
    • (2001) Mol Genet Genomics , vol.265 , Issue.4 , pp. 596-603
    • Thomas, N.A.1    Pawson, C.T.2    Jarrell, K.F.3
  • 104
    • 0034882854 scopus 로고    scopus 로고
    • The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum
    • 10.1046/j.1365-2958.2001.02542.x, 11532133
    • Patenge N, Berendes A, Engelhardt H, Schuster SC, Oesterhelt D. The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum. Mol Microbiol 2001, 41(3):653-663. 10.1046/j.1365-2958.2001.02542.x, 11532133.
    • (2001) Mol Microbiol , vol.41 , Issue.3 , pp. 653-663
    • Patenge, N.1    Berendes, A.2    Engelhardt, H.3    Schuster, S.C.4    Oesterhelt, D.5
  • 105
    • 0030058179 scopus 로고    scopus 로고
    • Isolation and characterization of flagella and flagellin proteins from the thermoacidophilic archaea Thermoplasma volcanium and Sulfolobus shibatae
    • 177742, 8550530
    • Faguy DM, Bayley DP, Kostyukova AS, Thomas NA, Jarrell KF. Isolation and characterization of flagella and flagellin proteins from the thermoacidophilic archaea Thermoplasma volcanium and Sulfolobus shibatae. J Bacteriol 1996, 178(3):902-905. 177742, 8550530.
    • (1996) J Bacteriol , vol.178 , Issue.3 , pp. 902-905
    • Faguy, D.M.1    Bayley, D.P.2    Kostyukova, A.S.3    Thomas, N.A.4    Jarrell, K.F.5
  • 106
    • 57749182669 scopus 로고    scopus 로고
    • The Structure of F-Pili
    • 10.1016/j.jmb.2008.10.054, 2650733, 18992755
    • Wang YA, Yu X, Silverman PM, Harris RL, Egelman EH. The Structure of F-Pili. J Mol Biol 2009, 385(1):22-29. 10.1016/j.jmb.2008.10.054, 2650733, 18992755.
    • (2009) J Mol Biol , vol.385 , Issue.1 , pp. 22-29
    • Wang, Y.A.1    Yu, X.2    Silverman, P.M.3    Harris, R.L.4    Egelman, E.H.5
  • 110
    • 67649576309 scopus 로고    scopus 로고
    • Community genomic and proteomic analyses of chemoautotrophic iron-oxidizing " Leptospirillum rubarum" (Group II) and " Leptospirillum ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms
    • 10.1128/AEM.02943-08, 2704813, 19429552
    • Goltsman DSA, Denef VJ, Singer SW, VerBerkmoes NC, Lefsrud M, Mueller RS, Dick GJ, Sun CL, Wheeler KE, Zemla A, et al. Community genomic and proteomic analyses of chemoautotrophic iron-oxidizing " Leptospirillum rubarum" (Group II) and " Leptospirillum ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms. Appl Environ Microbiol 2009, 75(13):4599-4615. 10.1128/AEM.02943-08, 2704813, 19429552.
    • (2009) Appl Environ Microbiol , vol.75 , Issue.13 , pp. 4599-4615
    • Goltsman, D.S.A.1    Denef, V.J.2    Singer, S.W.3    VerBerkmoes, N.C.4    Lefsrud, M.5    Mueller, R.S.6    Dick, G.J.7    Sun, C.L.8    Wheeler, K.E.9    Zemla, A.10
  • 111
    • 43149115851 scopus 로고    scopus 로고
    • Velvet: Algorithms for de novo short read assembly using de Bruijn graphs
    • 10.1101/gr.074492.107, 2336801, 18349386
    • Zerbino DR, Birney E. Velvet: Algorithms for de novo short read assembly using de Bruijn graphs. Genome Res 2008, 18(5):821-829. 10.1101/gr.074492.107, 2336801, 18349386.
    • (2008) Genome Res , vol.18 , Issue.5 , pp. 821-829
    • Zerbino, D.R.1    Birney, E.2
  • 112
    • 0031955116 scopus 로고    scopus 로고
    • Consed: A graphical tool for sequence finishing
    • 10.1101/gr.8.3.195, 9521923
    • Gordon D, Abajian C, Green P. Consed: A graphical tool for sequence finishing. Genome Res 1998, 8(3):195-202. 10.1101/gr.8.3.195, 9521923.
    • (1998) Genome Res , vol.8 , Issue.3 , pp. 195-202
    • Gordon, D.1    Abajian, C.2    Green, P.3
  • 113
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • 10.1093/bib/bbn013, 18372315
    • Katoh K, Toh H. Recent developments in the MAFFT multiple sequence alignment program. Brief Bioinform 2008, 9(4):286-298. 10.1093/bib/bbn013, 18372315.
    • (2008) Brief Bioinform , vol.9 , Issue.4 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 114
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
    • 10.1093/nar/gkf436, 135756, 12136088
    • Katoh K, Misawa K, Kuma K, Miyata T. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res 2002, 30(14):3059-3066. 10.1093/nar/gkf436, 135756, 12136088.
    • (2002) Nucleic Acids Res , vol.30 , Issue.14 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 115
    • 77949718257 scopus 로고    scopus 로고
    • FastTree 2-Approximately maximum-likelihood trees for large alignments
    • 10.1371/journal.pone.0009490, 2835736, 20224823
    • Price MN, Dehal PS, Arkin AP. FastTree 2-Approximately maximum-likelihood trees for large alignments. PLoS One 2010, 5(3):e9490. 10.1371/journal.pone.0009490, 2835736, 20224823.
    • (2010) PLoS One , vol.5 , Issue.3
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 116
    • 67649327176 scopus 로고    scopus 로고
    • FastTree: Computing large minimum evolution trees with profiles instead of a distance matrix
    • 10.1093/molbev/msp077, 2693737, 19377059
    • Price MN, Dehal PS, Arkin AP. FastTree: Computing large minimum evolution trees with profiles instead of a distance matrix. Mol Biol Evol 2009, 26(7):1641-1650. 10.1093/molbev/msp077, 2693737, 19377059.
    • (2009) Mol Biol Evol , vol.26 , Issue.7 , pp. 1641-1650
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 117
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • 10.1093/bioinformatics/btl446, 16928733
    • Stamatakis A. RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 2006, 22(21):2688-2690. 10.1093/bioinformatics/btl446, 16928733.
    • (2006) Bioinformatics , vol.22 , Issue.21 , pp. 2688-2690
    • Stamatakis, A.1
  • 118
    • 13444266488 scopus 로고    scopus 로고
    • A simple and fast secondary structure prediction method using hidden neural networks
    • 10.1093/bioinformatics/bth487, 15377504
    • Lin K, Simossis VA, Taylor WR, Heringa J. A simple and fast secondary structure prediction method using hidden neural networks. Bioinformatics 2005, 21(2):152-159. 10.1093/bioinformatics/bth487, 15377504.
    • (2005) Bioinformatics , vol.21 , Issue.2 , pp. 152-159
    • Lin, K.1    Simossis, V.A.2    Taylor, W.R.3    Heringa, J.4
  • 119
    • 0035834117 scopus 로고    scopus 로고
    • Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
    • 10.1073/pnas.211429998, 59822, 11593006
    • Drennan CL, Heo JY, Sintchak MD, Schreiter E, Ludden PW. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc Natl Acad Sci USA 2001, 98(21):11973-11978. 10.1073/pnas.211429998, 59822, 11593006.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.21 , pp. 11973-11978
    • Drennan, C.L.1    Heo, J.Y.2    Sintchak, M.D.3    Schreiter, E.4    Ludden, P.W.5


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