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Volumn 49, Issue 25, 2010, Pages 5390-5396

The temperature dependence of the kinetic isotope effects of dihydrofolate reductase from thermotoga maritima is influenced by intersubunit interactions

Author keywords

[No Author keywords available]

Indexed keywords

CHARGED RESIDUES; CONFORMATIONAL ENSEMBLE; DIHYDROFOLATE; DIHYDROFOLATE REDUCTASE; DIMER INTERFACE; HIGH THERMAL STABILITY; HOMODIMERS; HYDRIDE TRANSFERS; HYDROPHOBIC CORE; HYPERTHERMOPHILES; INTERSUBUNIT INTERACTION; KINETIC ISOTOPE EFFECTS; MELTING TEMPERATURES; OPPOSITE CHARGE; PROTEIN MOTION; REACTION COORDINATES; SALT BRIDGES; SIDE CHAINS; TEMPERATURE DEPENDENCE; THERMAL STABILITY; THERMOTOGA MARITIMA;

EID: 77953879146     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100761x     Document Type: Article
Times cited : (17)

References (53)
  • 1
    • 65549106864 scopus 로고    scopus 로고
    • Probing coupled motions in enzymatic hydrogen tunnelling reactions
    • Allemann, R. K., Evans, R. M., and Loveridge, E. J. (2009) Probing coupled motions in enzymatic hydrogen tunnelling reactions Biochem. Soc. Trans. 37, 349-353
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 349-353
    • Allemann, R.K.1    Evans, R.M.2    Loveridge, E.J.3
  • 3
    • 33645836711 scopus 로고    scopus 로고
    • Biochemistry: Enzyme motions inside and out
    • Benkovic, S. J. and Hammes-Schiffer, S. (2006) Biochemistry: Enzyme motions inside and out Science 312, 208-209
    • (2006) Science , vol.312 , pp. 208-209
    • Benkovic, S.J.1    Hammes-Schiffer, S.2
  • 4
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr, D. D., McElheny, D., Dyson, H. J., and Wright, P. E. (2006) The dynamic energy landscape of dihydrofolate reductase catalysis Science 313, 1638-1642
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 5
    • 61449179228 scopus 로고    scopus 로고
    • Dynamic Dysfunction in Dihydrofolate Reductase Results from Antifolate Drug Binding: Modulation of Dynamics within a Structural State
    • Mauldin, R. V., Carroll, M. J., and Lee, A. L. (2009) Dynamic Dysfunction in Dihydrofolate Reductase Results from Antifolate Drug Binding: Modulation of Dynamics within a Structural State Structure 17, 386-394
    • (2009) Structure , vol.17 , pp. 386-394
    • Mauldin, R.V.1    Carroll, M.J.2    Lee, A.L.3
  • 6
    • 33744953427 scopus 로고    scopus 로고
    • Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase
    • Iwakura, M., Maki, K., Takahashi, H., Takenawa, T., Yokota, A., Katayanagi, K., Kamiyama, T., and Gekko, K. (2006) Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase J. Biol. Chem. 281, 13234-13246
    • (2006) J. Biol. Chem. , vol.281 , pp. 13234-13246
    • Iwakura, M.1    Maki, K.2    Takahashi, H.3    Takenawa, T.4    Yokota, A.5    Katayanagi, K.6    Kamiyama, T.7    Gekko, K.8
  • 7
    • 34249104188 scopus 로고    scopus 로고
    • The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies
    • Liu, H. B. and Warshel, A. (2007) The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies Biochemistry 46, 6011-6025
    • (2007) Biochemistry , vol.46 , pp. 6011-6025
    • Liu, H.B.1    Warshel, A.2
  • 9
    • 0034737320 scopus 로고    scopus 로고
    • The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability
    • Dams, T., Auerbach, G., Bader, G., Jacob, U., Ploom, T., Huber, R., and Jaenicke, R. (2000) The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability J. Mol. Biol. 297, 659-672
    • (2000) J. Mol. Biol. , vol.297 , pp. 659-672
    • Dams, T.1    Auerbach, G.2    Bader, G.3    Jacob, U.4    Ploom, T.5    Huber, R.6    Jaenicke, R.7
  • 10
    • 0345647102 scopus 로고    scopus 로고
    • Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability
    • Dams, T., Bohm, G., Auerbach, G., Bader, G., Schurig, H., and Jaenicke, R. (1998) Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability Biol. Chem. 379, 367-371
    • (1998) Biol. Chem. , vol.379 , pp. 367-371
    • Dams, T.1    Bohm, G.2    Auerbach, G.3    Bader, G.4    Schurig, H.5    Jaenicke, R.6
  • 11
    • 0033551438 scopus 로고    scopus 로고
    • Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima
    • Dams, T. and Jaenicke, R. (1999) Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima Biochemistry 38, 9169-9178
    • (1999) Biochemistry , vol.38 , pp. 9169-9178
    • Dams, T.1    Jaenicke, R.2
  • 12
    • 0041761262 scopus 로고    scopus 로고
    • Hydride transfer during catalysis by dihydrofolate reductase from Thermotoga maritima
    • Maglia, G., Javed, M. H., and Allemann, R. K. (2003) Hydride transfer during catalysis by dihydrofolate reductase from Thermotoga maritima Biochem. J. 374, 529-535
    • (2003) Biochem. J. , vol.374 , pp. 529-535
    • Maglia, G.1    Javed, M.H.2    Allemann, R.K.3
  • 13
    • 67649610422 scopus 로고    scopus 로고
    • Effect of Dimerisation on the Stability and Catalytic Activity of Dihydrofolate Reductase from the Hyperthermophile Thermotoga maritima
    • Loveridge, E. J., Rodriguez, R. J., Swanwick, R. S., and Allemann, R. K. (2009) Effect of Dimerisation on the Stability and Catalytic Activity of Dihydrofolate Reductase from the Hyperthermophile Thermotoga maritima Biochemistry 48, 5922-5933
    • (2009) Biochemistry , vol.48 , pp. 5922-5933
    • Loveridge, E.J.1    Rodriguez, R.J.2    Swanwick, R.S.3    Allemann, R.K.4
  • 14
    • 70350561103 scopus 로고    scopus 로고
    • The Role of Arginine 28 in Catalysis by Dihydrofolate Reductase from the Hyperthermophile Thermotoga maritima
    • Loveridge, E. J., Maglia, G., and Allemann, R. K. (2009) The Role of Arginine 28 in Catalysis by Dihydrofolate Reductase from the Hyperthermophile Thermotoga maritima ChemBioChem 10, 2624-2627
    • (2009) ChemBioChem , vol.10 , pp. 2624-2627
    • Loveridge, E.J.1    Maglia, G.2    Allemann, R.K.3
  • 15
    • 33745362450 scopus 로고    scopus 로고
    • Hydride transfer reaction catalyzed by hyperthermophilic dihydrofolate reductase is dominated by quantum mechanical tunneling and is promoted by both inter- and intramonomeric correlated motions
    • Pang, J. Y., Pu, J. Z., Gao, J. L., Truhlar, D. G., and Allemann, R. K. (2006) Hydride transfer reaction catalyzed by hyperthermophilic dihydrofolate reductase is dominated by quantum mechanical tunneling and is promoted by both inter- and intramonomeric correlated motions J. Am. Chem. Soc. 128, 8015-8023
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8015-8023
    • Pang, J.Y.1    Pu, J.Z.2    Gao, J.L.3    Truhlar, D.G.4    Allemann, R.K.5
  • 16
    • 0034654087 scopus 로고    scopus 로고
    • Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima
    • Thoma, R., Hennig, M., Sterner, R., and Kirschner, K. (2000) Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima Struct. Folding Des. 8, 265-276
    • (2000) Struct. Folding Des. , vol.8 , pp. 265-276
    • Thoma, R.1    Hennig, M.2    Sterner, R.3    Kirschner, K.4
  • 17
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability
    • Vieille, C. and Zeikus, G. J. (2001) Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability Microbiol. Mol. Biol. Rev. 65, 1-43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 18
    • 30844449653 scopus 로고    scopus 로고
    • Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: Lessons from structural genomics of Thermotoga maritima
    • Robinson-Rechavi, M., Alibes, A., and Godzik, A. (2006) Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: Lessons from structural genomics of Thermotoga maritima J. Mol. Biol. 356, 547-557
    • (2006) J. Mol. Biol. , vol.356 , pp. 547-557
    • Robinson-Rechavi, M.1    Alibes, A.2    Godzik, A.3
  • 19
    • 0344848664 scopus 로고    scopus 로고
    • The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges
    • Merz, A., Knöchel, T., Jansonius, J. N., and Kirschner, K. (1999) The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges J. Mol. Biol. 288, 753-763
    • (1999) J. Mol. Biol. , vol.288 , pp. 753-763
    • Merz, A.1    Knöchel, T.2    Jansonius, J.N.3    Kirschner, K.4
  • 20
    • 0031565980 scopus 로고    scopus 로고
    • Disruption of an ionic network leads to accelerated thermal denaturation of d -glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima
    • Pappenberger, G., Schurig, H., and Jaenicke, R. (1997) Disruption of an ionic network leads to accelerated thermal denaturation of d -glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima J. Mol. Biol. 274, 676-683
    • (1997) J. Mol. Biol. , vol.274 , pp. 676-683
    • Pappenberger, G.1    Schurig, H.2    Jaenicke, R.3
  • 21
    • 69449095076 scopus 로고    scopus 로고
    • A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone reductase
    • Binter, A., Staunig, N., Jelesarov, I., Lohner, K., Palfey, B. A., Deller, S., Gruber, K., and Macheroux, P. (2009) A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone reductase FEBS J. 276, 5263-5274
    • (2009) FEBS J. , vol.276 , pp. 5263-5274
    • Binter, A.1    Staunig, N.2    Jelesarov, I.3    Lohner, K.4    Palfey, B.A.5    Deller, S.6    Gruber, K.7    MacHeroux, P.8
  • 22
    • 0032581344 scopus 로고    scopus 로고
    • Ion Pairs Involved in Maintaining a Thermostable Structure of Glutamate Dehydrogenase from a Hyperthermophilic Archaeon
    • Rahman, R. N. Z. A., Fujiwara, S., Nakamura, H., Takagi, M., and Imanaka, T. (1998) Ion Pairs Involved in Maintaining a Thermostable Structure of Glutamate Dehydrogenase from a Hyperthermophilic Archaeon Biochem. Biophys. Res. Commun. 248, 920-926
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 920-926
    • Rahman, R.N.Z.A.1    Fujiwara, S.2    Nakamura, H.3    Takagi, M.4    Imanaka, T.5
  • 24
    • 77749255402 scopus 로고    scopus 로고
    • Biochemical and Structural Properties of C imeras Constructed by Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases from Thermophilic and Mesophilic Microorganisms
    • Goihberg, E., Peretz, M., Tel-Or, S., Dym, O., Shimon, L., Frolow, F., and Burstein, Y. (2010) Biochemical and Structural Properties of Chimeras Constructed by Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases from Thermophilic and Mesophilic Microorganisms Biochemistry 49, 1943-1953
    • (2010) Biochemistry , vol.49 , pp. 1943-1953
    • Goihberg, E.1    Peretz, M.2    Tel-Or, S.3    Dym, O.4    Shimon, L.5    Frolow, F.6    Burstein, Y.7
  • 25
    • 33846889293 scopus 로고    scopus 로고
    • Molecular dynamics simulation of thermal unfolding of Thermatoga maritima DHFR
    • Pang, J. Y. and Allemann, R. K. (2007) Molecular dynamics simulation of thermal unfolding of Thermatoga maritima DHFR Phys. Chem. Chem. Phys. 9, 711-718
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 711-718
    • Pang, J.Y.1    Allemann, R.K.2
  • 26
    • 36949079198 scopus 로고
    • Crystalline dihydropteroylglutamic acid
    • Blakley, R. L. (1960) Crystalline dihydropteroylglutamic acid Nature 188, 231-232
    • (1960) Nature , vol.188 , pp. 231-232
    • Blakley, R.L.1
  • 27
    • 32944457660 scopus 로고    scopus 로고
    • Coupling of protein motions and hydrogen transfer during catalysis by Escherichia coli dihydrofolate reductase
    • Swanwick, R. S., Maglia, G., Tey, L., and Allemann, R. K. (2006) Coupling of protein motions and hydrogen transfer during catalysis by Escherichia coli dihydrofolate reductase Biochem. J. 394, 259-265
    • (2006) Biochem. J. , vol.394 , pp. 259-265
    • Swanwick, R.S.1    Maglia, G.2    Tey, L.3    Allemann, R.K.4
  • 29
    • 0020466628 scopus 로고
    • Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli
    • Stone, S. R. and Morrison, J. F. (1982) Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli Biochemistry 21, 3757-3765
    • (1982) Biochemistry , vol.21 , pp. 3757-3765
    • Stone, S.R.1    Morrison, J.F.2
  • 30
    • 0023668190 scopus 로고
    • Construction and Evaluation of the Kinetic Scheme Associated with Dihydrofolate Reductase from Escherichia coli
    • Fierke, C. A., Johnson, K. A., and Benkovic, S. J. (1987) Construction and Evaluation of the Kinetic Scheme Associated with Dihydrofolate Reductase from Escherichia coli Biochemistry 26, 4085-4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 31
    • 0242267579 scopus 로고    scopus 로고
    • Evidence for environmentally coupled hydrogen tunneling during dihydrofolate reductase catalysis
    • Maglia, G. and Allemann, R. K. (2003) Evidence for environmentally coupled hydrogen tunneling during dihydrofolate reductase catalysis J. Am. Chem. Soc. 125, 13372-13373
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13372-13373
    • Maglia, G.1    Allemann, R.K.2
  • 32
    • 56749083652 scopus 로고    scopus 로고
    • Solvent Effects on Environmentally Coupled Hydrogen Tunnelling during Catalysis by Dihydrofolate Reductase from Thermotoga maritima
    • Loveridge, E. J., Evans, R. M., and Allemann, R. K. (2008) Solvent Effects on Environmentally Coupled Hydrogen Tunnelling During Catalysis by Dihydrofolate Reductase from Thermotoga maritima Chem. - Eur. J. 14, 10782-10788
    • (2008) Chem. - Eur. J. , vol.14 , pp. 10782-10788
    • Loveridge, E.J.1    Evans, R.M.2    Allemann, R.K.3
  • 33
    • 76149110500 scopus 로고    scopus 로고
    • Solvent Effects on Catalysis by Escherichia coli Dihydrofolate Reductase
    • Loveridge, E. J., Tey, L. H., and Allemann, R. K. (2010) Solvent Effects on Catalysis by Escherichia coli Dihydrofolate Reductase J. Am. Chem. Soc. 132, 1137-1143
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1137-1143
    • Loveridge, E.J.1    Tey, L.H.2    Allemann, R.K.3
  • 35
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling: Linking catalysis to dynamics
    • Knapp, M. J. and Klinman, J. P. (2002) Environmentally coupled hydrogen tunneling: Linking catalysis to dynamics Eur. J. Biochem. 269, 3113-3121
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3113-3121
    • Knapp, M.J.1    Klinman, J.P.2
  • 36
    • 33748601471 scopus 로고    scopus 로고
    • Tunneling and dynamics in enzymatic hydride transfer
    • Nagel, Z. D. and Klinman, J. P. (2006) Tunneling and dynamics in enzymatic hydride transfer Chem. Rev. 106, 3095-3118
    • (2006) Chem. Rev. , vol.106 , pp. 3095-3118
    • Nagel, Z.D.1    Klinman, J.P.2
  • 37
    • 0036305396 scopus 로고    scopus 로고
    • A new conceptual framework for enzyme catalysis: Hydrogen tunneling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes
    • Sutcliffe, M. J. and Scrutton, N. S. (2002) A new conceptual framework for enzyme catalysis: Hydrogen tunneling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes Eur. J. Biochem. 269, 3096-3102
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3096-3102
    • Sutcliffe, M.J.1    Scrutton, N.S.2
  • 39
    • 10044273966 scopus 로고    scopus 로고
    • Promoting Vibrations in Human Purine Nucleoside Phosphorylase. A Molecular Dynamics and Hybrid Quantum Mechanical/Molecular Mechanical Study
    • Nunez, S., Antoniou, D., Schramm, V. L., and Schwartz, S. D. (2004) Promoting Vibrations in Human Purine Nucleoside Phosphorylase. A Molecular Dynamics and Hybrid Quantum Mechanical/Molecular Mechanical Study J. Am. Chem. Soc. 126, 15720-15729
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15720-15729
    • Nunez, S.1    Antoniou, D.2    Schramm, V.L.3    Schwartz, S.D.4
  • 41
    • 72249089538 scopus 로고    scopus 로고
    • Evidence to Support the Hypothesis That Promoting Vibrations Enhance the Rate of an Enzyme Catalyzed H-Tunneling Reaction
    • Pudney, C. R., Hay, S., Levy, C., Pang, J., Sutcliffe, M. J., Leys, D., and Scrutton, N. S. (2009) Evidence To Support the Hypothesis That Promoting Vibrations Enhance the Rate of an Enzyme Catalyzed H-Tunneling Reaction J. Am. Chem. Soc. 131, 17072-17073
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17072-17073
    • Pudney, C.R.1    Hay, S.2    Levy, C.3    Pang, J.4    Sutcliffe, M.J.5    Leys, D.6    Scrutton, N.S.7
  • 43
    • 1842531419 scopus 로고    scopus 로고
    • Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: The altered structure of a mutant enzyme may form the basis of its diminished catalytic performance
    • Swanwick, R. S., Shrimpton, P. J., and Allemann, R. K. (2004) Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: The altered structure of a mutant enzyme may form the basis of its diminished catalytic performance Biochemistry 43, 4119-4127
    • (2004) Biochemistry , vol.43 , pp. 4119-4127
    • Swanwick, R.S.1    Shrimpton, P.J.2    Allemann, R.K.3
  • 44
    • 0037188007 scopus 로고    scopus 로고
    • Nuclear quantum effects and enzyme dynamics in dihydrofolate reductase catalysis
    • Agarwal, P. K., Billeter, S. R., and Hammes-Schiffer, S. (2002) Nuclear quantum effects and enzyme dynamics in dihydrofolate reductase catalysis J. Phys. Chem. B 106, 3283-3293
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3283-3293
    • Agarwal, P.K.1    Billeter, S.R.2    Hammes-Schiffer, S.3
  • 45
    • 0344391945 scopus 로고    scopus 로고
    • Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase
    • Garcia-Viloca, M., Truhlar, D. G., and Gao, J. (2003) Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase Biochemistry 42, 13558-13575
    • (2003) Biochemistry , vol.42 , pp. 13558-13575
    • Garcia-Viloca, M.1    Truhlar, D.G.2    Gao, J.3
  • 46
    • 6344294816 scopus 로고    scopus 로고
    • The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase
    • Thorpe, I. F. and Brooks, C. L. (2004) The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase Proteins 57, 444-457
    • (2004) Proteins , vol.57 , pp. 444-457
    • Thorpe, I.F.1    Brooks, C.L.2
  • 47
    • 25144458498 scopus 로고    scopus 로고
    • Conformational substates modulate hydride transfer in dihydrofolate reductase
    • Thorpe, I. F. and Brooks, C. L. (2005) Conformational substates modulate hydride transfer in dihydrofolate reductase J. Am. Chem. Soc. 127, 12997-13006
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12997-13006
    • Thorpe, I.F.1    Brooks, C.L.2
  • 48
    • 71749090188 scopus 로고    scopus 로고
    • The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer
    • Pijning, T., van Pouderoyen, G., Kluskens, L., van der Oost, J., and Dijkstra, B. W. (2009) The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer FEBS Lett. 583, 3665-3670
    • (2009) FEBS Lett. , vol.583 , pp. 3665-3670
    • Pijning, T.1    Van Pouderoyen, G.2    Kluskens, L.3    Van Der Oost, J.4    Dijkstra, B.W.5
  • 49
    • 77953886948 scopus 로고    scopus 로고
    • http://cmr.jcvi.org/cgi-bin/CMR/GenomePage.cgi?org=nttp02.
  • 50
    • 33645313846 scopus 로고    scopus 로고
    • Chromosome evolution in the Thermotogales: Large-scale inversions and strain diversification of CRISPR sequences
    • DeBoy, R. T., Mongodin, E. F., Emerson, J. B., and Nelson, K. E. (2006) Chromosome evolution in the Thermotogales: Large-scale inversions and strain diversification of CRISPR sequences J. Bacteriol. 188, 2364-2374
    • (2006) J. Bacteriol. , vol.188 , pp. 2364-2374
    • Deboy, R.T.1    Mongodin, E.F.2    Emerson, J.B.3    Nelson, K.E.4
  • 51
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °c
    • Huber, R., Langworthy, T. A., König, H., Thomm, M., Woese, C. R., Sleytr, U. B., and Stetter, K. O. (1986) Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °C Arch. Microbiol. 144, 324-333
    • (1986) Arch. Microbiol. , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    König, H.3    Thomm, M.4    Woese, C.R.5    Sleytr, U.B.6    Stetter, K.O.7
  • 52
    • 0001218383 scopus 로고
    • Thermotoga neapolitana sp. nov. of the extremely thermophilic, eubacterial genus Thermotoga
    • Jannasch, H. W., Huber, R., Belkin, S., and Stetter, K. O. (1988) Thermotoga neapolitana sp. nov. of the extremely thermophilic, eubacterial genus Thermotoga Arch. Microbiol. 150, 103-104
    • (1988) Arch. Microbiol. , vol.150 , pp. 103-104
    • Jannasch, H.W.1    Huber, R.2    Belkin, S.3    Stetter, K.O.4
  • 53
    • 0034815472 scopus 로고    scopus 로고
    • Thermotoga petrophila sp. nov. and Thermotoga naphthophila sp. nov., two hyperthermophilic bacteria from the Kubiki oil reservoir in Niigata, Japan
    • Takahata, Y., Nishijima, M., Hoaki, T., and Maruyama, T. (2001) Thermotoga petrophila sp. nov. and Thermotoga naphthophila sp. nov., two hyperthermophilic bacteria from the Kubiki oil reservoir in Niigata, Japan Int. J. Syst. Evol. Microbiol. 51, 1901-1909
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 1901-1909
    • Takahata, Y.1    Nishijima, M.2    Hoaki, T.3    Maruyama, T.4


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