메뉴 건너뛰기




Volumn 75, Issue 14, 2009, Pages 4835-4852

Complete genome sequence of the chemolithoautotrophic marine magnetotactic coccus strain MC-1

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL STRAINS; BIOCHEMICAL PATHWAY; CARBON METABOLISM; CHEMOLITHOAUTOTROPHIC; COMPLETE GENOMES; GLUCONEOGENESIS; HETEROTROPHIC GROWTH; MAGNETOTACTIC BACTERIA; MARINE BACTERIUM; PROTEOBACTERIA;

EID: 67650445451     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02874-08     Document Type: Article
Times cited : (95)

References (121)
  • 1
    • 0028282042 scopus 로고
    • Protein histidine kinases and signal transduction in prokaryotes and eukaryotes
    • Alex, L. A., and M. I. Simon. 1994. Protein histidine kinases and signal transduction in prokaryotes and eukaryotes. Trends Genet. 10:133-138.
    • (1994) Trends Genet , vol.10 , pp. 133-138
    • Alex, L.A.1    Simon, M.I.2
  • 3
    • 0037424274 scopus 로고    scopus 로고
    • A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1
    • Arakaki, A., J. Webb, and T. Matsunaga. 2003. A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1. J. Biol. Chem. 278:8745-8750.
    • (2003) J. Biol. Chem , vol.278 , pp. 8745-8750
    • Arakaki, A.1    Webb, J.2    Matsunaga, T.3
  • 4
    • 0032900737 scopus 로고    scopus 로고
    • CRITICA: Coding region identification tool invoking comparative analysis
    • Badger, J. H., and G. J. Olsen. 1999. CRITICA: coding region identification tool invoking comparative analysis. Mol. Biol. Evol. 16:512-524.
    • (1999) Mol. Biol. Evol , vol.16 , pp. 512-524
    • Badger, J.H.1    Olsen, G.J.2
  • 5
    • 0018880142 scopus 로고
    • Ultrastructure of a magnetotactic spirillum
    • Balkwill, D. L., D. Maratea, and R. P. Blakemore. 1980. Ultrastructure of a magnetotactic spirillum. J. Bacteriol. 141:1399-1408.
    • (1980) J. Bacteriol , vol.141 , pp. 1399-1408
    • Balkwill, D.L.1    Maratea, D.2    Blakemore, R.P.3
  • 6
    • 0035928778 scopus 로고    scopus 로고
    • The shxVW locus is essential for oxidation of inorganic sulfur and molecular hydrogen by Paracoccus pantotrophus GB17: A novel function for lithotrophy
    • Bardischewsky, F., and C. G. Friedrich. 2001. The shxVW locus is essential for oxidation of inorganic sulfur and molecular hydrogen by Paracoccus pantotrophus GB17: a novel function for lithotrophy. FEMS Microbiol. Lett. 202:215-220.
    • (2001) FEMS Microbiol. Lett , vol.202 , pp. 215-220
    • Bardischewsky, F.1    Friedrich, C.G.2
  • 7
    • 33645467197 scopus 로고    scopus 로고
    • The flavoprotein SoxF functions in chemotrophic thiosulfate oxidation of Paracoccus pantotrophus in vivo and in vitro
    • Bardischewsky, F., A. Quentmeier, and C. G. Friedrich. 2006. The flavoprotein SoxF functions in chemotrophic thiosulfate oxidation of Paracoccus pantotrophus in vivo and in vitro. FEMS Microbiol. Lett. 258:121-126.
    • (2006) FEMS Microbiol. Lett , vol.258 , pp. 121-126
    • Bardischewsky, F.1    Quentmeier, A.2    Friedrich, C.G.3
  • 8
    • 0000511901 scopus 로고
    • Structure and function of the bacterial magnetosome
    • Bazylinski, D. A. 1995. Structure and function of the bacterial magnetosome. ASM News 61:337-343.
    • (1995) ASM News , vol.61 , pp. 337-343
    • Bazylinski, D.A.1
  • 9
    • 0000051606 scopus 로고
    • Denitrification and assimilatory nitrate reduction in Aquaspirillum magnetotacticum
    • Bazylinski, D. A., and R. P. Blakemore. 1983. Denitrification and assimilatory nitrate reduction in Aquaspirillum magnetotacticum. Appl. Environ. Microbiol. 46:1118-1124.
    • (1983) Appl. Environ. Microbiol , vol.46 , pp. 1118-1124
    • Bazylinski, D.A.1    Blakemore, R.P.2
  • 10
    • 0021071492 scopus 로고
    • Nitrogen-fixation (acetylene-reduction) in Aquaspirillum magnetotacticum
    • Bazylinski, D. A., and R. P. Blakemore. 1983. Nitrogen-fixation (acetylene-reduction) in Aquaspirillum magnetotacticum. Curr. Microbiol. 9:305-308.
    • (1983) Curr. Microbiol , vol.9 , pp. 305-308
    • Bazylinski, D.A.1    Blakemore, R.P.2
  • 13
    • 34548480456 scopus 로고    scopus 로고
    • Controlled biomineralization by and applications of magnetotactic bacteria
    • Bazylinski, D. A., and S. Schübbe. 2007. Controlled biomineralization by and applications of magnetotactic bacteria. Adv. Appl. Microbiol. 62:21-62.
    • (2007) Adv. Appl. Microbiol , vol.62 , pp. 21-62
    • Bazylinski, D.A.1    Schübbe, S.2
  • 14
    • 67650498239 scopus 로고    scopus 로고
    • Bazylinski, D. A., and T. J. Williams. 2007. Ecophysiology of magnetotactic bacteria, p. 37-75. In D. Schüler (ed.), Magnetoreception and magnetosomes in bacteria, 3. Springer, Berlin, Germany.
    • Bazylinski, D. A., and T. J. Williams. 2007. Ecophysiology of magnetotactic bacteria, p. 37-75. In D. Schüler (ed.), Magnetoreception and magnetosomes in bacteria, vol. 3. Springer, Berlin, Germany.
  • 15
    • 14644401764 scopus 로고    scopus 로고
    • The complete denitrification pathway of the symbiotic, nitrogen-fixing bacterium Bradyrhizobium japonicum
    • Bedmar, E. J., E. F. Robles, and M. J. Delgado. 2005. The complete denitrification pathway of the symbiotic, nitrogen-fixing bacterium Bradyrhizobium japonicum. Biochem. Soc. Trans. 33:141-144.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 141-144
    • Bedmar, E.J.1    Robles, E.F.2    Delgado, M.J.3
  • 19
    • 0016717082 scopus 로고
    • Magnetotactic bacteria
    • Blakemore, R. 1975. Magnetotactic bacteria. Science 190:377-379.
    • (1975) Science , vol.190 , pp. 377-379
    • Blakemore, R.1
  • 20
  • 21
    • 0022220946 scopus 로고
    • Microaerobic conditions are required for magnetite formation within Aquaspirillum magnetotacticum
    • Blakemore, R. P., K. A. Short, D. A. Bazylinski, C. Rosenblatt, and R. B. Frankel. 1985. Microaerobic conditions are required for magnetite formation within Aquaspirillum magnetotacticum. Geomicrobiol. J. 4:53-71.
    • (1985) Geomicrobiol. J , vol.4 , pp. 53-71
    • Blakemore, R.P.1    Short, K.A.2    Bazylinski, D.A.3    Rosenblatt, C.4    Frankel, R.B.5
  • 22
    • 33749431828 scopus 로고    scopus 로고
    • Prophage Finder: A prophage loci prediction tool for prokaryotic genome sequences
    • Bose, M., and R. D. Barber. 2006. Prophage Finder: a prophage loci prediction tool for prokaryotic genome sequences. In Silico Biol. 6:223-227.
    • (2006) In Silico Biol , vol.6 , pp. 223-227
    • Bose, M.1    Barber, R.D.2
  • 23
    • 0035156057 scopus 로고    scopus 로고
    • Transcriptional activation of Bordetella alcaligin siderophore genes requires the AlcR regulator with alcaligin as inducer
    • Brickman, T. J., H. Y. Kang, and S. K. Armstrong. 2001. Transcriptional activation of Bordetella alcaligin siderophore genes requires the AlcR regulator with alcaligin as inducer. J. Bacteriol. 183:483-489.
    • (2001) J. Bacteriol , vol.183 , pp. 483-489
    • Brickman, T.J.1    Kang, H.Y.2    Armstrong, S.K.3
  • 24
    • 0037825641 scopus 로고    scopus 로고
    • Prophages and bacterial genomics: What have we learned so far?
    • Casjens, S. 2003. Prophages and bacterial genomics: what have we learned so far? Mol. Microbiol. 49:277-300.
    • (2003) Mol. Microbiol , vol.49 , pp. 277-300
    • Casjens, S.1
  • 27
    • 84898703263 scopus 로고    scopus 로고
    • Organization and elemental analysis of P-, S-, and Fe-rich inclusions in a population of freshwater magnetococci
    • Cox, B. L., R. Popa, D. A. Bazylinski, B. Lanoil, S. Douglas, A. Belz, D. L. Engler, and K. H. Nealson. 2002. Organization and elemental analysis of P-, S-, and Fe-rich inclusions in a population of freshwater magnetococci. Geomicrobiol. J. 19:387-406.
    • (2002) Geomicrobiol. J , vol.19 , pp. 387-406
    • Cox, B.L.1    Popa, R.2    Bazylinski, D.A.3    Lanoil, B.4    Douglas, S.5    Belz, A.6    Engler, D.L.7    Nealson, K.H.8
  • 28
    • 14544272337 scopus 로고    scopus 로고
    • Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum
    • Dahl, C., S. Engels, A. S. Pott-Sperling, A. Schulte, J. Sander, Y. Lübbe, O. Deuster, and D. C. Brune. 2005. Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum. J. Bacteriol. 187:1392-1404.
    • (2005) J. Bacteriol , vol.187 , pp. 1392-1404
    • Dahl, C.1    Engels, S.2    Pott-Sperling, A.S.3    Schulte, A.4    Sander, J.5    Lübbe, Y.6    Deuster, O.7    Brune, D.C.8
  • 29
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • D'Andrea, L. D., and L. Regan. 2003. TPR proteins: the versatile helix. Trends Biochem. Sci. 28:655-662.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 30
    • 35648963623 scopus 로고    scopus 로고
    • ABC transporters: How small machines do a big job
    • Davidson, A. L., and P. C. Maloney. 2007. ABC transporters: how small machines do a big job. Trends Microbiol. 15:448-455.
    • (2007) Trends Microbiol , vol.15 , pp. 448-455
    • Davidson, A.L.1    Maloney, P.C.2
  • 31
    • 0032833172 scopus 로고    scopus 로고
    • Genome analysis of several marine, magnetotactic bacterial strains by pulsed-field gel electrophoresis
    • Dean, A. J., and D. A. Bazylinski. 1999. Genome analysis of several marine, magnetotactic bacterial strains by pulsed-field gel electrophoresis. Curr. Microbiol. 39:219-225.
    • (1999) Curr. Microbiol , vol.39 , pp. 219-225
    • Dean, A.J.1    Bazylinski, D.A.2
  • 33
    • 0346252346 scopus 로고    scopus 로고
    • The Bradyrhizobium japonicum napEDABC genes encoding the periplasmic nitrate reductase are essential for nitrate respiration
    • Delgado, M. J., N. Bonnard, A. Tresierra-Ayala, E. J. Bedmar, and P. Müller. 2003. The Bradyrhizobium japonicum napEDABC genes encoding the periplasmic nitrate reductase are essential for nitrate respiration. Microbiology 149:3395-3403.
    • (2003) Microbiology , vol.149 , pp. 3395-3403
    • Delgado, M.J.1    Bonnard, N.2    Tresierra-Ayala, A.3    Bedmar, E.J.4    Müller, P.5
  • 34
    • 0027511449 scopus 로고
    • Multiple evolutionary origins of magnetotaxis in bacteria
    • DeLong, E. F., R. B. Frankel, and D. A. Bazylinski. 1993. Multiple evolutionary origins of magnetotaxis in bacteria. Science 259:803-806.
    • (1993) Science , vol.259 , pp. 803-806
    • DeLong, E.F.1    Frankel, R.B.2    Bazylinski, D.A.3
  • 36
    • 4844224403 scopus 로고    scopus 로고
    • Evidence for a copper-dependent iron transport system in the marine, magnetotactic bacterium strain MV-1
    • Dubbels, B. L., A. A. DiSpirito, J. D. Morton, J. D. Semrau, J. N. Neto, and D. A. Bazylinski. 2004. Evidence for a copper-dependent iron transport system in the marine, magnetotactic bacterium strain MV-1. Microbiology 150:2931-2945.
    • (2004) Microbiology , vol.150 , pp. 2931-2945
    • Dubbels, B.L.1    DiSpirito, A.A.2    Morton, J.D.3    Semrau, J.D.4    Neto, J.N.5    Bazylinski, D.A.6
  • 37
    • 2942607685 scopus 로고    scopus 로고
    • A memory-efficient dynamic programming algorithm for optimal alignment of a sequence to an RNA secondary structure
    • Eddy, S. R. 2002. A memory-efficient dynamic programming algorithm for optimal alignment of a sequence to an RNA secondary structure. BMC Bioinformatics 3:18.
    • (2002) BMC Bioinformatics , vol.3 , pp. 18
    • Eddy, S.R.1
  • 38
    • 20444472906 scopus 로고    scopus 로고
    • Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus
    • Epel, B., K. O. Schäfer, A. Quentmeier, C. Friedrich, and W. Lubitz. 2005. Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus. J. Biol. Inorg. Chem. 10:636-642.
    • (2005) J. Biol. Inorg. Chem , vol.10 , pp. 636-642
    • Epel, B.1    Schäfer, K.O.2    Quentmeier, A.3    Friedrich, C.4    Lubitz, W.5
  • 39
    • 34547793558 scopus 로고    scopus 로고
    • The origin of mitochondria in light of a fluid prokaryotic chromosome model
    • Esser, C., W. Martin, and T. Dagan. 2007. The origin of mitochondria in light of a fluid prokaryotic chromosome model. Biol. Lett. 3:180-184.
    • (2007) Biol. Lett , vol.3 , pp. 180-184
    • Esser, C.1    Martin, W.2    Dagan, T.3
  • 40
    • 0031978181 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. II. Error probabilities
    • Ewing, B., and P. Green. 1998. Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res. 8:186-194.
    • (1998) Genome Res , vol.8 , pp. 186-194
    • Ewing, B.1    Green, P.2
  • 41
    • 0031955518 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. I. Accuracy assessment
    • Ewing, B., L. Hillier, M. C. Wendl, and P. Green. 1998. Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res. 8:175-185.
    • (1998) Genome Res , vol.8 , pp. 175-185
    • Ewing, B.1    Hillier, L.2    Wendl, M.C.3    Green, P.4
  • 42
    • 0025197439 scopus 로고
    • Magnetic iron-sulfur crystals from a magnetotactic microorganism
    • Farina, M., D. M. S. Esquivel, and H. G. P. Lins de Barros. 1990. Magnetic iron-sulfur crystals from a magnetotactic microorganism. Nature 343:256-258.
    • (1990) Nature , vol.343 , pp. 256-258
    • Farina, M.1    Esquivel, D.M.S.2    Lins de Barros, H.G.P.3
  • 43
    • 15244339397 scopus 로고    scopus 로고
    • Diversity and vertical distribution of magnetotactic bacteria along chemical gradients in freshwater microcosms
    • Flies, C. B., H. M. Jonkers, D. de Beer, K. Bosselmann, M. E. Böttcher, and D. Schüler. 2005. Diversity and vertical distribution of magnetotactic bacteria along chemical gradients in freshwater microcosms. FEMS Microbiol. Ecol. 52:185-195.
    • (2005) FEMS Microbiol. Ecol , vol.52 , pp. 185-195
    • Flies, C.B.1    Jonkers, H.M.2    de Beer, D.3    Bosselmann, K.4    Böttcher, M.E.5    Schüler, D.6
  • 45
    • 0037436089 scopus 로고    scopus 로고
    • Envelope ultrastructure of uncultured naturally occurring magnetotactic cocci
    • Freitas, F., C. N. Keim, B. Kachar, M. Farina, and U. Lins. 2003. Envelope ultrastructure of uncultured naturally occurring magnetotactic cocci. FEMS Microbiol. Lett. 219:33-38.
    • (2003) FEMS Microbiol. Lett , vol.219 , pp. 33-38
    • Freitas, F.1    Keim, C.N.2    Kachar, B.3    Farina, M.4    Lins, U.5
  • 46
    • 38349117475 scopus 로고    scopus 로고
    • Diversity and distribution of hemerythrin-like proteins in prokaryotes
    • French, C. E., J. M. Bell, and F. B. Ward. 2008. Diversity and distribution of hemerythrin-like proteins in prokaryotes. FEMS Microbiol. Lett. 279:131-145.
    • (2008) FEMS Microbiol. Lett , vol.279 , pp. 131-145
    • French, C.E.1    Bell, J.M.2    Ward, F.B.3
  • 48
    • 31444443960 scopus 로고    scopus 로고
    • Dynamic analysis of a genomic island in Magnetospirillum sp. strain AMB-1 reveals how magnetosome synthesis developed
    • Fukuda, Y., Y. Okamura, H. Takeyama, and T. Matsunaga. 2006. Dynamic analysis of a genomic island in Magnetospirillum sp. strain AMB-1 reveals how magnetosome synthesis developed. FEBS Lett. 580:801-812.
    • (2006) FEBS Lett , vol.580 , pp. 801-812
    • Fukuda, Y.1    Okamura, Y.2    Takeyama, H.3    Matsunaga, T.4
  • 49
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v. 2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy, J. L., M. R. Laird, F. Chen, S. Rey, C. J. Walsh, M. Ester, and F. S. Brinkman. 2005. PSORTb v. 2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21:617-623.
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5    Ester, M.6    Brinkman, F.S.7
  • 50
    • 0023954501 scopus 로고
    • Characterization of the bacterial magnetosome membrane
    • Gorby, Y. A., T. J. Beveridge, and R. P. Blakemore. 1988. Characterization of the bacterial magnetosome membrane. J. Bacteriol. 170:834-841.
    • (1988) J. Bacteriol , vol.170 , pp. 834-841
    • Gorby, Y.A.1    Beveridge, T.J.2    Blakemore, R.P.3
  • 51
    • 0031955116 scopus 로고    scopus 로고
    • Consed: A graphical tool for sequence finishing
    • Gordon, D., C. Abajian, and P. Green. 1998. Consed: a graphical tool for sequence finishing. Genome Res. 8:195-202.
    • (1998) Genome Res , vol.8 , pp. 195-202
    • Gordon, D.1    Abajian, C.2    Green, P.3
  • 52
    • 14644413601 scopus 로고    scopus 로고
    • A genomic island present along the bacterial chromosome of the Parachlamydiaceae UWE25, an obligate amoebal endosymbiont, encodes a potentially functional F-like conjugative DNA transfer system
    • Greub, G., F. Collyn, L. Guy, and C. A. Roten. 2004. A genomic island present along the bacterial chromosome of the Parachlamydiaceae UWE25, an obligate amoebal endosymbiont, encodes a potentially functional F-like conjugative DNA transfer system. BMC Microbiol. 4:48.
    • (2004) BMC Microbiol , vol.4 , pp. 48
    • Greub, G.1    Collyn, F.2    Guy, L.3    Roten, C.A.4
  • 54
    • 0035486722 scopus 로고    scopus 로고
    • A large gene cluster encoding several magnetosome proteins is conserved in different species of magnetotactic bacteria
    • Grünberg, K., C. Wawer, B. M. Tebo, and D. Schüler. 2001. A large gene cluster encoding several magnetosome proteins is conserved in different species of magnetotactic bacteria. Appl. Environ. Microbiol. 67:4573-4582.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 4573-4582
    • Grünberg, K.1    Wawer, C.2    Tebo, B.M.3    Schüler, D.4
  • 56
    • 33749989029 scopus 로고    scopus 로고
    • Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum
    • Hensen, D., D. Sperling, H. G. Trüper, D. C. Brune, and C. Dahl. 2006. Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum. Mol. Microbiol. 62:794-810.
    • (2006) Mol. Microbiol , vol.62 , pp. 794-810
    • Hensen, D.1    Sperling, D.2    Trüper, H.G.3    Brune, D.C.4    Dahl, C.5
  • 57
    • 0038236515 scopus 로고    scopus 로고
    • Growth and magnetosome formation by microaerophilic Magnetospirillum strains in an oxygen-controlled fermentor
    • Heyen, U., and D. Schüler. 2003. Growth and magnetosome formation by microaerophilic Magnetospirillum strains in an oxygen-controlled fermentor. Appl. Microbiol. Biotechnol. 61:536-544.
    • (2003) Appl. Microbiol. Biotechnol , vol.61 , pp. 536-544
    • Heyen, U.1    Schüler, D.2
  • 58
    • 33746661497 scopus 로고    scopus 로고
    • Structural basis for O2 sensing by the hemerythrin-like domain of a bacterial chemotaxis protein: Substrate tunnel and fluxional N terminus
    • Isaza, C. E., R. Silaghi-Dumitrescu, R. B. Iyer, D. M. Kurtz, Jr., and M. K. Chan. 2006. Structural basis for O2 sensing by the hemerythrin-like domain of a bacterial chemotaxis protein: substrate tunnel and fluxional N terminus. Biochemistry 45:9023-9031.
    • (2006) Biochemistry , vol.45 , pp. 9023-9031
    • Isaza, C.E.1    Silaghi-Dumitrescu, R.2    Iyer, R.B.3    Kurtz Jr., D.M.4    Chan, M.K.5
  • 59
    • 32544451343 scopus 로고    scopus 로고
    • Evolution of the soluble nitrate reductase: Defining the monomeric periplasmic nitrate reductase subgroup
    • Jepson, B. J., A. Marietou, S. Mohan, J. A. Cole, C. S. Butler, and D. J. Richardson. 2006. Evolution of the soluble nitrate reductase: defining the monomeric periplasmic nitrate reductase subgroup. Biochem. Soc. Trans. 34:122-126.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 122-126
    • Jepson, B.J.1    Marietou, A.2    Mohan, S.3    Cole, J.A.4    Butler, C.S.5    Richardson, D.J.6
  • 60
    • 65349149041 scopus 로고    scopus 로고
    • Comparative analysis of magnetosome gene clusters in magnetotactic bacteria provides further evidence for horizontal gene transfer
    • Jogler, C., M. Kube, S. Schübbe, S. Ullrich, H. Teeling, D. A. Bazylinski, R. Reinhardt, and D. Schüler. 2009. Comparative analysis of magnetosome gene clusters in magnetotactic bacteria provides further evidence for horizontal gene transfer. Environ. Microbiol. 11:1267-1277.
    • (2009) Environ. Microbiol , vol.11 , pp. 1267-1277
    • Jogler, C.1    Kube, M.2    Schübbe, S.3    Ullrich, S.4    Teeling, H.5    Bazylinski, D.A.6    Reinhardt, R.7    Schüler, D.8
  • 61
    • 67650503507 scopus 로고    scopus 로고
    • Jogler, C., and D. Schüler. 2007. Genetic analysis of magnetosome biomineralization, p. 133-161. In D. Schüler (ed.), Magnetoreception and magnetosomes in bacteria, 3. Springer, Berlin, Germany.
    • Jogler, C., and D. Schüler. 2007. Genetic analysis of magnetosome biomineralization, p. 133-161. In D. Schüler (ed.), Magnetoreception and magnetosomes in bacteria, vol. 3. Springer, Berlin, Germany.
  • 62
    • 18944380045 scopus 로고    scopus 로고
    • Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath)
    • Karlsen, O. A., L. Ramsevik, L. J. Bruseth, O. Larsen, A. Brenner, F. S. Berven, H. B. Jensen, and J. R. Lillehaug. 2005. Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath). FEBS J. 272:2428-2440.
    • (2005) FEBS J , vol.272 , pp. 2428-2440
    • Karlsen, O.A.1    Ramsevik, L.2    Bruseth, L.J.3    Larsen, O.4    Brenner, A.5    Berven, F.S.6    Jensen, H.B.7    Lillehaug, J.R.8
  • 63
    • 33751213049 scopus 로고    scopus 로고
    • Spatial organization of the bacterial chemotaxis system
    • Kentner, D., and V. Sourjik. 2006. Spatial organization of the bacterial chemotaxis system. Curr. Opin. Microbiol. 9:619-624.
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 619-624
    • Kentner, D.1    Sourjik, V.2
  • 64
    • 0028949531 scopus 로고
    • Heliobacterium modesticaldum, sp. nov., a thermophilic heliobacterium of hot springs and volcanic soils
    • Kimble, L. K., L. Mandelco, C. R. Woese, and M. T. Madigan. 1995. Heliobacterium modesticaldum, sp. nov., a thermophilic heliobacterium of hot springs and volcanic soils. Arch. Microbiol. 163:259-267.
    • (1995) Arch. Microbiol , vol.163 , pp. 259-267
    • Kimble, L.K.1    Mandelco, L.2    Woese, C.R.3    Madigan, M.T.4
  • 65
    • 34548506889 scopus 로고    scopus 로고
    • Cell biology of magnetosome formation
    • D. Schüler ed, Springer, Berlin, Germany
    • Komeili, A. 2007. Cell biology of magnetosome formation, p. 163-174. In D. Schüler (ed.), Magnetoreception and magnetosomes in bacteria, vol. 3. Springer, Berlin, Germany.
    • (2007) Magnetoreception and magnetosomes in bacteria , vol.3 , pp. 163-174
    • Komeili, A.1
  • 66
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili, A., Z. Li, D. K. Newman, and G. J. Jensen. 2006. Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311:242-245.
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 67
    • 1642406025 scopus 로고    scopus 로고
    • Magnetosome vesicles are present before magnetite formation, and MamA is required for their activation
    • Komeili, A., H. Vali, T. J. Beveridge, and D. K. Newman. 2004. Magnetosome vesicles are present before magnetite formation, and MamA is required for their activation. Proc. Natl. Acad. Sci. USA 101:3839-3844.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3839-3844
    • Komeili, A.1    Vali, H.2    Beveridge, T.J.3    Newman, D.K.4
  • 68
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., B. Larsson, G. von Heijne, and E. L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 69
    • 34248669001 scopus 로고    scopus 로고
    • Functional specialization within the Fur family of metalloregulators
    • Lee, J.-W., and J. D. Helmann. 2007. Functional specialization within the Fur family of metalloregulators. Biometals 20:485-499.
    • (2007) Biometals , vol.20 , pp. 485-499
    • Lee, J.-W.1    Helmann, J.D.2
  • 70
    • 67149095570 scopus 로고    scopus 로고
    • Isolation and characterization of a magnetotactic bacterial culture from the Mediterranean Sea. Environ
    • Epub ahead of print, doi:10.1111/ j.1462-2920.2009.01887.x
    • Lefèvre, C. T., A. Bernadac, K. Yu-Zhang, N. Pradel, and L.-F. Wu. 2009. Isolation and characterization of a magnetotactic bacterial culture from the Mediterranean Sea. Environ. Microbiol. [Epub ahead of print.] doi:10.1111/ j.1462-2920.2009.01887.x.
    • (2009) Microbiol
    • Lefèvre, C.T.1    Bernadac, A.2    Yu-Zhang, K.3    Pradel, N.4    Wu, L.-F.5
  • 71
    • 0039005906 scopus 로고    scopus 로고
    • Electron spectroscopic imaging of magnetotactic bacteria: Magnetosome morphology and diversity
    • Lins, U., F. Freitas, C. N. Keim, and M. Farina. 2000. Electron spectroscopic imaging of magnetotactic bacteria: magnetosome morphology and diversity. Microsc. Microanal. 6:463-470.
    • (2000) Microsc. Microanal , vol.6 , pp. 463-470
    • Lins, U.1    Freitas, F.2    Keim, C.N.3    Farina, M.4
  • 72
    • 0030854739 scopus 로고    scopus 로고
    • tRNAscan-SE: A program for improved detection of transfer RNA genes in genomic sequence
    • Lowe, T. M., and S. R. Eddy. 1997. tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res. 25:955-964.
    • (1997) Nucleic Acids Res , vol.25 , pp. 955-964
    • Lowe, T.M.1    Eddy, S.R.2
  • 73
    • 0033604287 scopus 로고    scopus 로고
    • Similarly organized lysogeny modules in temperate Siphoviridae from low GC content gram-positive bacteria
    • Lucchini, S., F. Desiere, and H. Brüssow. 1999. Similarly organized lysogeny modules in temperate Siphoviridae from low GC content gram-positive bacteria. Virology 263:427-435.
    • (1999) Virology , vol.263 , pp. 427-435
    • Lucchini, S.1    Desiere, F.2    Brüssow, H.3
  • 74
    • 0027339446 scopus 로고
    • Role of the sigma 70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli
    • Makino, K., M. Amemura, S. K. Kim, A. Nakata, and H. Shinagawa. 1993. Role of the sigma 70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli. Genes Dev. 7:149-160.
    • (1993) Genes Dev , vol.7 , pp. 149-160
    • Makino, K.1    Amemura, M.2    Kim, S.K.3    Nakata, A.4    Shinagawa, H.5
  • 75
    • 0023801563 scopus 로고
    • Regulation of the phosphate regulon of Escherichia coli. Activation of pstS transcription by PhoB protein in vitro
    • Makino, K., H. Shinagawa, M. Amemura, S. Kimura, A. Nakata, and A. Ishihama. 1988. Regulation of the phosphate regulon of Escherichia coli. Activation of pstS transcription by PhoB protein in vitro. J. Mol. Biol. 203:85-95.
    • (1988) J. Mol. Biol , vol.203 , pp. 85-95
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Kimura, S.4    Nakata, A.5    Ishihama, A.6
  • 78
    • 27844484656 scopus 로고    scopus 로고
    • Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1
    • Matsunaga, T., Y. Okamura, Y. Fukuda, A. T. Wahyudi, Y. Murase, and H. Takeyama. 2005. Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1. DNA Res. 12:157-166.
    • (2005) DNA Res , vol.12 , pp. 157-166
    • Matsunaga, T.1    Okamura, Y.2    Fukuda, Y.3    Wahyudi, A.T.4    Murase, Y.5    Takeyama, H.6
  • 79
    • 0028822799 scopus 로고
    • An iron-regulated gene, magA, encoding an iron transport protein of Magnetospirillum sp. strain AMB-1
    • Nakamura, C., J. G. Burgess, K. Sode, and T. Matsunaga. 1995. An iron-regulated gene, magA, encoding an iron transport protein of Magnetospirillum sp. strain AMB-1. J. Biol. Chem. 270:28392-28396.
    • (1995) J. Biol. Chem , vol.270 , pp. 28392-28396
    • Nakamura, C.1    Burgess, J.G.2    Sode, K.3    Matsunaga, T.4
  • 80
    • 39749141534 scopus 로고    scopus 로고
    • The AraC-family regulator GadX enhances multidrug resistance in Escherichia coli by activating expression of mdtEF multidrug efflux genes
    • Nishino, K., Y. Senda, and A. Yamaguchi. 2008. The AraC-family regulator GadX enhances multidrug resistance in Escherichia coli by activating expression of mdtEF multidrug efflux genes. J. Infect. Chemother. 14:23-29.
    • (2008) J. Infect. Chemother , vol.14 , pp. 23-29
    • Nishino, K.1    Senda, Y.2    Yamaguchi, A.3
  • 81
    • 0032958117 scopus 로고    scopus 로고
    • Iron reductase for magnetite synthesis in the magnetotactic bacterium Magnetospirillum magnetotacticum
    • Noguchi, Y., T. Fujiwara, K. Yoshimatsu, and Y. Fukumori. 1999. Iron reductase for magnetite synthesis in the magnetotactic bacterium Magnetospirillum magnetotacticum. J. Bacteriol. 181:2142-2147.
    • (1999) J. Bacteriol , vol.181 , pp. 2142-2147
    • Noguchi, Y.1    Fujiwara, T.2    Yoshimatsu, K.3    Fukumori, Y.4
  • 82
    • 0034604396 scopus 로고    scopus 로고
    • Paulsen, I. T., L. Nguyen, M. K. Sliwinski, R. Rabus, and M. H. Saier, Jr. 2000. Microbial genome analyses: comparative transport capabilities in eighteen prokaryotes. J. Mol. Biol. 301:75-100.
    • Paulsen, I. T., L. Nguyen, M. K. Sliwinski, R. Rabus, and M. H. Saier, Jr. 2000. Microbial genome analyses: comparative transport capabilities in eighteen prokaryotes. J. Mol. Biol. 301:75-100.
  • 83
    • 0033571287 scopus 로고    scopus 로고
    • Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12
    • Potter, L. C., and J. A. Cole. 1999. Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12. Biochem. J. 344:69-76.
    • (1999) Biochem. J , vol.344 , pp. 69-76
    • Potter, L.C.1    Cole, J.A.2
  • 84
    • 0344495378 scopus 로고    scopus 로고
    • Sulfur oxidation in Paracoccus pantotrophus: Interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein
    • Quentmeier, A., P. Hellwig, F. Bardischewsky, G. Grelle, R. Kraft, and C. G. Friedrich. 2003. Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein. Biochem. Biophys. Res. Commun. 312:1011-1018.
    • (2003) Biochem. Biophys. Res. Commun , vol.312 , pp. 1011-1018
    • Quentmeier, A.1    Hellwig, P.2    Bardischewsky, F.3    Grelle, G.4    Kraft, R.5    Friedrich, C.G.6
  • 85
    • 8744255663 scopus 로고    scopus 로고
    • Sulfide dehydrogenase activity of the monomeric flavoprotein SoxF of Paracoccus pantotrophus
    • Quentmeier, A., P. Hellwig, F. Bardischewsky, R. Wichmann, and C. G. Friedrich. 2004. Sulfide dehydrogenase activity of the monomeric flavoprotein SoxF of Paracoccus pantotrophus. Biochemistry 43:14696-14703.
    • (2004) Biochemistry , vol.43 , pp. 14696-14703
    • Quentmeier, A.1    Hellwig, P.2    Bardischewsky, F.3    Wichmann, R.4    Friedrich, C.G.5
  • 86
    • 55449113709 scopus 로고    scopus 로고
    • Comparative analyses of fundamental differences in membrane transport capabilities in prokaryotes and eukaryotes
    • Ren, Q., and I. T. Paulsen. 2005. Comparative analyses of fundamental differences in membrane transport capabilities in prokaryotes and eukaryotes. PLoS Comput. Biol. 1:e27.
    • (2005) PLoS Comput. Biol , vol.1
    • Ren, Q.1    Paulsen, I.T.2
  • 87
    • 38549158363 scopus 로고    scopus 로고
    • Think big-giant genes in bacteria
    • Reva, O., and B. Tümmler. 2008. Think big-giant genes in bacteria. Environ. Microbiol. 10:768-777.
    • (2008) Environ. Microbiol , vol.10 , pp. 768-777
    • Reva, O.1    Tümmler, B.2
  • 88
  • 89
    • 34347392111 scopus 로고    scopus 로고
    • Comparative genome analysis of four magnetotactic bacteria reveals a complex set of group-specific genes implicated in magnetosome biomineralization and function
    • Richter, M., M. Kube, D. A. Bazylinski, T. Lombardot, F. O. Glöckner, R. Reinhardt, and D. Schüler. 2007. Comparative genome analysis of four magnetotactic bacteria reveals a complex set of group-specific genes implicated in magnetosome biomineralization and function. J. Bacteriol. 189:4899-4910.
    • (2007) J. Bacteriol , vol.189 , pp. 4899-4910
    • Richter, M.1    Kube, M.2    Bazylinski, D.A.3    Lombardot, T.4    Glöckner, F.O.5    Reinhardt, R.6    Schüler, D.7
  • 90
    • 0034111671 scopus 로고    scopus 로고
    • The complete genomic sequence of the marine phage Roseophage SIO1 shares homology with nonmarine phages
    • Rohwer, F., A. Segall, G. Steward, V. Seguritan, M. Breitbart, F. Wolven, and F. Azam. 2000. The complete genomic sequence of the marine phage Roseophage SIO1 shares homology with nonmarine phages. Limnol. Oceanogr. 45:408-418.
    • (2000) Limnol. Oceanogr , vol.45 , pp. 408-418
    • Rohwer, F.1    Segall, A.2    Steward, G.3    Seguritan, V.4    Breitbart, M.5    Wolven, F.6    Azam, F.7
  • 91
    • 22644438480 scopus 로고    scopus 로고
    • C-di-GMP: The dawning of a novel bacterial signaling system
    • Romling, U., M. Gomelsky, and M. Y. Galperin. 2005. C-di-GMP: the dawning of a novel bacterial signaling system. Mol. Microbiol. 57:629-639.
    • (2005) Mol. Microbiol , vol.57 , pp. 629-639
    • Romling, U.1    Gomelsky, M.2    Galperin, M.Y.3
  • 92
    • 33644763960 scopus 로고    scopus 로고
    • An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria
    • Scheffel, A., M. Gruska, D. Faivre, A. Linaroudis, J. M. Plitzko, and D. Schüler. 2006. An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria. Nature 440:110-114.
    • (2006) Nature , vol.440 , pp. 110-114
    • Scheffel, A.1    Gruska, M.2    Faivre, D.3    Linaroudis, A.4    Plitzko, J.M.5    Schüler, D.6
  • 93
    • 34548492254 scopus 로고    scopus 로고
    • The acidic repetitive domain of the Magnetospirillum gryphiswaldense MamJ protein displays hypervariability but is not required for magnetosome chain assembly
    • Scheffel, A., and D. Schüler. 2007. The acidic repetitive domain of the Magnetospirillum gryphiswaldense MamJ protein displays hypervariability but is not required for magnetosome chain assembly. J. Bacteriol. 189:6437-6446.
    • (2007) J. Bacteriol , vol.189 , pp. 6437-6446
    • Scheffel, A.1    Schüler, D.2
  • 94
    • 17344383176 scopus 로고    scopus 로고
    • Characterization of a spontaneous nonmagnetic mutant of Magnetospirillum gryphiswaldense reveals a large deletion comprising a putative magnetosome island
    • Schübbe, S., M. Kube, A. Scheffel, C. Wawer, U. Heyen, A. Meyerdierks, M. H. Madkour, F. Mayer, R. Reinhardt, and D. Schüler. 2003. Characterization of a spontaneous nonmagnetic mutant of Magnetospirillum gryphiswaldense reveals a large deletion comprising a putative magnetosome island. J. Bacteriol. 185:5779-5790.
    • (2003) J. Bacteriol , vol.185 , pp. 5779-5790
    • Schübbe, S.1    Kube, M.2    Scheffel, A.3    Wawer, C.4    Heyen, U.5    Meyerdierks, A.6    Madkour, M.H.7    Mayer, F.8    Reinhardt, R.9    Schüler, D.10
  • 96
    • 0742269413 scopus 로고    scopus 로고
    • Molecular analysis of a subcellular compartment: The magnetosome membrane in Magnetospirillum gryphiswaldense
    • Schüler, D. 2004. Molecular analysis of a subcellular compartment: the magnetosome membrane in Magnetospirillum gryphiswaldense. Arch. Microbiol. 181:1-7.
    • (2004) Arch. Microbiol , vol.181 , pp. 1-7
    • Schüler, D.1
  • 97
    • 0031984106 scopus 로고    scopus 로고
    • 4 biomineralization during aerobic and microaerobic growth of Magnetospirillum gryphiswaldense
    • 4 biomineralization during aerobic and microaerobic growth of Magnetospirillum gryphiswaldense. J. Bacteriol. 180:159-162.
    • (1998) J. Bacteriol , vol.180 , pp. 159-162
    • Schüler, D.1    Baeuerlein, E.2
  • 98
    • 0029826049 scopus 로고    scopus 로고
    • Iron-limited growth and kinetics of iron uptake in Magnetospirillum gryphiswaldense
    • Schüler, D., and E. Baeuerlein. 1996. Iron-limited growth and kinetics of iron uptake in Magnetospirillum gryphiswaldense. Arch. Microbiol. 166:301-307.
    • (1996) Arch. Microbiol , vol.166 , pp. 301-307
    • Schüler, D.1    Baeuerlein, E.2
  • 99
    • 15344351224 scopus 로고    scopus 로고
    • The presumptive magnetosome protein Mms16 is a poly(3-hydroxybutyrate) granule-bound protein (phasin) in Magnetospirillum gryphiswaldense
    • Schultheiss, D., R. Handrick, D. Jendrossek, M. Hanzlik, and D. Schüler. 2005. The presumptive magnetosome protein Mms16 is a poly(3-hydroxybutyrate) granule-bound protein (phasin) in Magnetospirillum gryphiswaldense. J. Bacteriol. 187:2416-2425.
    • (2005) J. Bacteriol , vol.187 , pp. 2416-2425
    • Schultheiss, D.1    Handrick, R.2    Jendrossek, D.3    Hanzlik, M.4    Schüler, D.5
  • 100
    • 33845505324 scopus 로고    scopus 로고
    • Scott, K. M., S. M. Sievert, F. N. Abril, L. A. Ball, C. J. Barrett, R. A. Blake, A. J. Boller, P. S. Chain, J. A. Clark, C. R. Davis, C. Detter, K. F. Do, K. P. Dobrinski, B. I. Faza, K. A. Fitzpatrick, S. K. Freyermuth, T. L. Harmer, L. J. Hauser, M. Hügler, C. A. Kerfeld, M. G. Klotz, W. W. Kong, M. Land, A. Lapidus, F. W. Larimer, D. L. Longo, S. Lucas, S. A. Malfatti, S. E. Massey, D. D. Martin, Z. McCuddin, F. Meyer, J. L. Moore, L. H. Ocampo, Jr., J. H. Paul, I. T. Paulsen, D. K. Reep, Q. Ren, R. L. Ross, P. Y. Sato, P. Thomas, L. E. Tinkham, and G. T. Zeruth. 2006. The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena XCL-2. PLoS Biol. 4:e383.
    • Scott, K. M., S. M. Sievert, F. N. Abril, L. A. Ball, C. J. Barrett, R. A. Blake, A. J. Boller, P. S. Chain, J. A. Clark, C. R. Davis, C. Detter, K. F. Do, K. P. Dobrinski, B. I. Faza, K. A. Fitzpatrick, S. K. Freyermuth, T. L. Harmer, L. J. Hauser, M. Hügler, C. A. Kerfeld, M. G. Klotz, W. W. Kong, M. Land, A. Lapidus, F. W. Larimer, D. L. Longo, S. Lucas, S. A. Malfatti, S. E. Massey, D. D. Martin, Z. McCuddin, F. Meyer, J. L. Moore, L. H. Ocampo, Jr., J. H. Paul, I. T. Paulsen, D. K. Reep, Q. Ren, R. L. Ross, P. Y. Sato, P. Thomas, L. E. Tinkham, and G. T. Zeruth. 2006. The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena XCL-2. PLoS Biol. 4:e383.
  • 103
    • 4444239145 scopus 로고    scopus 로고
    • Smart, J. L., J. W. Willett, and C. E. Bauer. 2004. Regulation of hem gene expression in Rhodobacter capsulatus by redox and photosystem regulators RegA, CrtJ, FnrL, and AerR. J. Mol. Biol. 342:1171-1186.
    • Smart, J. L., J. W. Willett, and C. E. Bauer. 2004. Regulation of hem gene expression in Rhodobacter capsulatus by redox and photosystem regulators RegA, CrtJ, FnrL, and AerR. J. Mol. Biol. 342:1171-1186.
  • 104
    • 0026520954 scopus 로고
    • Phylogenetic diversity and identification of nonculturable magnetotactic bacteria
    • Spring, S., R. Amann, W. Ludwig, K. H. Schleifer, and N. Petersen. 1992. Phylogenetic diversity and identification of nonculturable magnetotactic bacteria. Syst. Appl. Microbiol. 15:116-122.
    • (1992) Syst. Appl. Microbiol , vol.15 , pp. 116-122
    • Spring, S.1    Amann, R.2    Ludwig, W.3    Schleifer, K.H.4    Petersen, N.5
  • 106
    • 0031887619 scopus 로고    scopus 로고
    • Phylogenetic affiliation and ultrastructure of uncultured magnetic bacteria with unusually large magnetosomes
    • Spring, S., U. Lins, R. Amann, K.-H. Schleifer, L. C. S. Ferreira, D. M. S. Esquivel, and M. Farina. 1998. Phylogenetic affiliation and ultrastructure of uncultured magnetic bacteria with unusually large magnetosomes. Arch. Microbiol. 169:136-147.
    • (1998) Arch. Microbiol , vol.169 , pp. 136-147
    • Spring, S.1    Lins, U.2    Amann, R.3    Schleifer, K.-H.4    Ferreira, L.C.S.5    Esquivel, D.M.S.6    Farina, M.7
  • 107
    • 0036523461 scopus 로고    scopus 로고
    • Evolution of nitrate reductase: Molecular and structural variations on a common function
    • Stolz, J. F., and P. Basu. 2002. Evolution of nitrate reductase: molecular and structural variations on a common function. Chembiochem 3:198-206.
    • (2002) Chembiochem , vol.3 , pp. 198-206
    • Stolz, J.F.1    Basu, P.2
  • 108
    • 43949129748 scopus 로고    scopus 로고
    • High-yield growth and magnetosome formation by Magnetospirillum gryphiswaldense MSR-1 in an oxygen-controlled fermentor supplied solely with air
    • Sun, J. B., F. Zhao, T. Tang, W. Jiang, J. S. Tian, Y. Li, and J. L. Li. 2008. High-yield growth and magnetosome formation by Magnetospirillum gryphiswaldense MSR-1 in an oxygen-controlled fermentor supplied solely with air. Appl. Microbiol. Biotechnol. 79:389-397.
    • (2008) Appl. Microbiol. Biotechnol , vol.79 , pp. 389-397
    • Sun, J.B.1    Zhao, F.2    Tang, T.3    Jiang, W.4    Tian, J.S.5    Li, Y.6    Li, J.L.7
  • 111
    • 27144485750 scopus 로고    scopus 로고
    • A hypervariable 130-kilobase genomic region of Magnetospirillum gryphiswaldense comprises a magnetosome island which undergoes frequent rearrangements during stationary growth
    • Ullrich, S., M. Kube, S. Schübbe, R. Reinhardt, and D. Schüler. 2005. A hypervariable 130-kilobase genomic region of Magnetospirillum gryphiswaldense comprises a magnetosome island which undergoes frequent rearrangements during stationary growth. J. Bacteriol. 187:7176-7184.
    • (2005) J. Bacteriol , vol.187 , pp. 7176-7184
    • Ullrich, S.1    Kube, M.2    Schübbe, S.3    Reinhardt, R.4    Schüler, D.5
  • 112
    • 0003338719 scopus 로고    scopus 로고
    • Phosphorous assimilation and control of the phosphate regulon
    • F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger ed, 2nd ed. ASM Press, Washington, DC
    • Wanner, B. L. 1996. Phosphorous assimilation and control of the phosphate regulon, p. 1357-1381. In F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 1357-1381
    • Wanner, B.L.1
  • 113
    • 33144458254 scopus 로고    scopus 로고
    • Evidence for autotrophy via the reverse tricarboxylic acid cycle in the marine magnetotactic coccus strain MC-1
    • Williams, T. J., C. L. Zhang, J. H. Scott, and D. A. Bazylinski. 2006. Evidence for autotrophy via the reverse tricarboxylic acid cycle in the marine magnetotactic coccus strain MC-1. Appl. Environ. Microbiol. 72: 1322-1329.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 1322-1329
    • Williams, T.J.1    Zhang, C.L.2    Scott, J.H.3    Bazylinski, D.A.4
  • 114
    • 55549133935 scopus 로고    scopus 로고
    • Williamson, S. J., S. C. Cary, K. E. Williamson, R. R. Helton, S. R. Bench, D. Winget, and K. E. Wommack. 2008. Lysogenic virus-host interactions predominate at deep-sea diffuse-flow hydrothermal vents. ISME J. 2:1112-1121.
    • Williamson, S. J., S. C. Cary, K. E. Williamson, R. R. Helton, S. R. Bench, D. Winget, and K. E. Wommack. 2008. Lysogenic virus-host interactions predominate at deep-sea diffuse-flow hydrothermal vents. ISME J. 2:1112-1121.
  • 116
    • 0034604416 scopus 로고    scopus 로고
    • Phosphate depletion in the western North Atlantic Ocean
    • Wu, J., W. Sunda, E. A. Boyle, and D. M. Karl. 2000. Phosphate depletion in the western North Atlantic Ocean. Science 289:759-762.
    • (2000) Science , vol.289 , pp. 759-762
    • Wu, J.1    Sunda, W.2    Boyle, E.A.3    Karl, D.M.4
  • 117
    • 19344378727 scopus 로고    scopus 로고
    • Wu, M., L. V. Sun, J. Vamathevan, M. Riegler, R. Deboy, J. C. Brownlie, E. A. McGraw, W. Martin, C. Esser, N. Ahmadinejad, C. Wiegand, R. Madupu, M. J. Beanan, L. M. Brinkac, S. C. Daugherty, A. S. Durkin, J. F. Kolonay, W. C. Nelson, Y. Mohamoud, P. Lee, K. Berry, M. B. Young, T. Utterback, J. Weidman, W. C. Nierman, I. T. Paulsen, K. E. Nelson, H. Tettelin, S. L. O'Neill, and J. A. Eisen. 2004. Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements. PLoS Biol. 2:e69.
    • Wu, M., L. V. Sun, J. Vamathevan, M. Riegler, R. Deboy, J. C. Brownlie, E. A. McGraw, W. Martin, C. Esser, N. Ahmadinejad, C. Wiegand, R. Madupu, M. J. Beanan, L. M. Brinkac, S. C. Daugherty, A. S. Durkin, J. F. Kolonay, W. C. Nelson, Y. Mohamoud, P. Lee, K. Berry, M. B. Young, T. Utterback, J. Weidman, W. C. Nierman, I. T. Paulsen, K. E. Nelson, H. Tettelin, S. L. O'Neill, and J. A. Eisen. 2004. Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements. PLoS Biol. 2:e69.
  • 118
    • 0034595406 scopus 로고    scopus 로고
    • A hemerythrin-like domain in a bacterial chemotaxis protein
    • Xiong, J., D. M. Kurtz, Jr., J. Ai, and J. Sanders-Loehr. 2000. A hemerythrin-like domain in a bacterial chemotaxis protein. Biochemistry 39:5117-5125.
    • (2000) Biochemistry , vol.39 , pp. 5117-5125
    • Xiong, J.1    Kurtz Jr., D.M.2    Ai, J.3    Sanders-Loehr, J.4
  • 119
    • 0028884619 scopus 로고
    • Nitrite reductase from the magnetotactic bacterium Magnetospirillum magnetotacticum. A novel cytochrome cd1 with Fe(II):nitrite oxidoreductase activity
    • Yamazaki, T., H. Oyanagi, T. Fujiwara, and Y. Fukumori. 1995. Nitrite reductase from the magnetotactic bacterium Magnetospirillum magnetotacticum. A novel cytochrome cd1 with Fe(II):nitrite oxidoreductase activity. Eur. J. Biochem. 233:665-671.
    • (1995) Eur. J. Biochem , vol.233 , pp. 665-671
    • Yamazaki, T.1    Oyanagi, H.2    Fujiwara, T.3    Fukumori, Y.4
  • 120
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox
    • Zhulin, I. B., B. L. Taylor, and R. Dixon. 1997. PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 22:331-333.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3
  • 121
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft, W. G. 1997. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61:533-616.
    • (1997) Microbiol. Mol. Biol. Rev , vol.61 , pp. 533-616
    • Zumft, W.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.