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Volumn 62, Issue 24, 2005, Pages 2974-2984

Microbial Life at high temperature, the challenges, the strategies

Author keywords

Archaea; Bacteria; Channeling; Extremophiles; Modified nucleosides; Thermophiles

Indexed keywords

NUCLEIC ACID; NUCLEOSIDE; TRANSFER RNA;

EID: 29344459635     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5251-8     Document Type: Review
Times cited : (37)

References (94)
  • 1
    • 0014501198 scopus 로고
    • Thermus aquaticus gen. n. and sp. n., a non-sporulating extreme thermophile
    • Brock T. D. and Freeze H. (1969) Thermus aquaticus gen. n. and sp. n., a non-sporulating extreme thermophile. J. Bacteriol. 98: 289-297
    • (1969) J. Bacteriol. , vol.98 , pp. 289-297
    • Brock, T.D.1    Freeze, H.2
  • 2
    • 0015275944 scopus 로고
    • Sulfolobus: A new genus of sulfur oxidizing bacteria living at low pH and high temperatures
    • Brock T. D., Brock K. M., Belly R. T. and Weiss R. L. (1972) Sulfolobus: a new genus of sulfur oxidizing bacteria living at low pH and high temperatures. Arch. Microbiol. 84: 54-68
    • (1972) Arch. Microbiol. , vol.84 , pp. 54-68
    • Brock, T.D.1    Brock, K.M.2    Belly, R.T.3    Weiss, R.L.4
  • 3
    • 0033768088 scopus 로고    scopus 로고
    • Towards the ecology of hyperthermophiles: Biotopes, new isolation strategies and novel metabolic properties
    • Huber R., Huber H. and Stetter K.O. (2000) Towards the ecology of hyperthermophiles: biotopes, new isolation strategies and novel metabolic properties. FEMS Microbiol. Rev. 24: 615-623
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 615-623
    • Huber, R.1    Huber, H.2    Stetter, K.O.3
  • 4
    • 0035931866 scopus 로고    scopus 로고
    • Life in extreme environments
    • Rothschild L. J. and Mancinelli R. L. (2001) Life in extreme environments. Nature 409: 1092-1101
    • (2001) Nature , vol.409 , pp. 1092-1101
    • Rothschild, L.J.1    Mancinelli, R.L.2
  • 5
    • 0034021526 scopus 로고    scopus 로고
    • Biomolecular stability and life at high temperatures
    • Daniel R. M. and Cowan D. A. (2000) Biomolecular stability and life at high temperatures. Cell. Mol. Life Sci. 57: 250-264
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 250-264
    • Daniel, R.M.1    Cowan, D.A.2
  • 6
    • 0032863453 scopus 로고    scopus 로고
    • DNA repair in Archaea: Mementos from the last universal common ancestor?
    • DiRuggiero J., Brown J. R., Bogert A. P. and Robb F. T. (1999) DNA repair in Archaea: mementos from the last universal common ancestor? J. Mol. Evol. 49: 474-484
    • (1999) J. Mol. Evol. , vol.49 , pp. 474-484
    • Diruggiero, J.1    Brown, J.R.2    Bogert, A.P.3    Robb, F.T.4
  • 7
    • 0033056563 scopus 로고    scopus 로고
    • The biochemical diversity of life near and above 100°C in marine environments
    • Adams M. W. W. (1999) The biochemical diversity of life near and above 100°C in marine environments. J. App. Microbiol. Symp. Suppl. 85: 108S-117S
    • (1999) J. App. Microbiol. Symp. Suppl. , vol.85
    • Adams, M.W.W.1
  • 8
    • 0037007636 scopus 로고    scopus 로고
    • A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont
    • Huber H., Hohn M. J., Rachel R., Fuchs T., Wimmer V. G. and Stetter, K. O. (2002) A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont. Nature, 417: 63-67
    • (2002) Nature , vol.417 , pp. 63-67
    • Huber, H.1    Hohn, M.J.2    Rachel, R.3    Fuchs, T.4    Wimmer, V.G.5    Stetter, K.O.6
  • 9
    • 0031061411 scopus 로고    scopus 로고
    • Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper limit of life to 113°C
    • Bloch E., Rachel R., Burggraf S., Hafenbrandl D., Jannasch H. and Stetter K. O. (1997) Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper limit of life to 113°C. Extremophiles 1: 14-21
    • (1997) Extremophiles , vol.1 , pp. 14-21
    • Bloch, E.1    Rachel, R.2    Burggraf, S.3    Hafenbrandl, D.4    Jannasch, H.5    Stetter, K.O.6
  • 10
    • 0042021865 scopus 로고    scopus 로고
    • Extending the upper temperature limit for life
    • Kashefi K. and Lovley D. (2003) Extending the upper temperature limit for life. Science 301: 934
    • (2003) Science , vol.301 , pp. 934
    • Kashefi, K.1    Lovley, D.2
  • 11
    • 0029832927 scopus 로고    scopus 로고
    • Perspectives on archaeal diversity, thermophily and monophyly from environmental rRNA sequences
    • USA
    • Barns S. M., Delwiche C. F., Palmers J. D. and Pace N. R. (1996) Perspectives on archaeal diversity, thermophily and monophyly from environmental rRNA sequences. Proc. Natl. Acad. Sci. USA 93: 9188-9193
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 9188-9193
    • Barns, S.M.1    Delwiche, C.F.2    Palmers, J.D.3    Pace, N.R.4
  • 12
    • 0025375817 scopus 로고
    • A comparison of thermal adaptations of membrane lipids in psychrophilic and thermophilic bacteria
    • Russel N. J. and Fukunaga N. (1990) A comparison of thermal adaptations of membrane lipids in psychrophilic and thermophilic bacteria. FEMS Microbiol. Rev. 75: 171-182
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 171-182
    • Russel, N.J.1    Fukunaga, N.2
  • 13
    • 0021809506 scopus 로고
    • The effect of growth temperature on the thermophilic behavior of the membranes of a thermophilic Bacillus. Composition-structure-function relationships
    • Reizer J., Grossowicz N. and Barenholz Y. (1985) The effect of growth temperature on the thermophilic behavior of the membranes of a thermophilic Bacillus. Composition-structure-function relationships. Biochim. Biophys. Acta 815: 268-280
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 268-280
    • Reizer, J.1    Grossowicz, N.2    Barenholz, Y.3
  • 14
    • 0001098191 scopus 로고
    • Effect of growth temperature on the lipid composition of two strains of Thermus sp.
    • Prado A., Da Costa M. S. and Madeira V. C. (1988) Effect of growth temperature on the lipid composition of two strains of Thermus sp. J. Gen. Microbiol. 134: 1653-1660
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1653-1660
    • Prado, A.1    Da Costa, M.S.2    Madeira, V.C.3
  • 15
    • 0022578265 scopus 로고
    • Structure, biosynthesis and physical properties of archaebacterial lipids
    • De Rosa M., Gambacorta A. and Gliozzi A. (1986) Structure, biosynthesis and physical properties of archaebacterial lipids. Mol. Microbiol. Rev. 50: 70-80
    • (1986) Mol. Microbiol. Rev. , vol.50 , pp. 70-80
    • De Rosa, M.1    Gambacorta, A.2    Gliozzi, A.3
  • 16
    • 77956822726 scopus 로고
    • Membrane lipids of Archaea
    • Kates M., Kushnen D. J. and Matheson A. T. (eds.), Elsevier, Amsterdam, Amsterdam
    • Kates M. (1993) Membrane lipids of Archaea. In: The Biochemistry of Archaea (Archaebacteria), pp. 261-295, Kates M., Kushnen D. J. and Matheson A. T. (eds.), Elsevier, Amsterdam, Amsterdam
    • (1993) The Biochemistry of Archaea (Archaebacteria) , pp. 261-295
    • Kates, M.1
  • 17
    • 0032142866 scopus 로고    scopus 로고
    • The essence of being extremophilic: The role of the unique archaeal membrane lipids
    • van de Vossenberg J., Driessen A. and Konings W. N. (1998) The essence of being extremophilic: the role of the unique archaeal membrane lipids. Extremophiles 2: 163-170
    • (1998) Extremophiles , vol.2 , pp. 163-170
    • Van De Vossenberg, J.1    Driessen, A.2    Konings, W.N.3
  • 19
    • 0026543822 scopus 로고
    • Functional reconstitution of membrane proteins in mono-layer liposomes from bipolar lipids in Sulfolobus acidocaldarius
    • Elferink M. G., De Wit J. G., Demel R., Driessen A. J. and Konings W. N. (1992) Functional reconstitution of membrane proteins in mono-layer liposomes from bipolar lipids in Sulfolobus acidocaldarius. J. Biol. Chem. 267: 1375-1381
    • (1992) J. Biol. Chem. , vol.267 , pp. 1375-1381
    • Elferink, M.G.1    De Wit, J.G.2    Demel, R.3    Driessen, A.J.4    Konings, W.N.5
  • 20
    • 0000869403 scopus 로고
    • Effect of isoprenoid cyclization on the transition temperature of lipids in thermophilic archaebacteria
    • Gliozi A., Paoli G., De Rosa M. and Gambbacorta A. (1983) Effect of isoprenoid cyclization on the transition temperature of lipids in thermophilic archaebacteria. Biochim. Biophys. Acta 735: 234-242
    • (1983) Biochim. Biophys. Acta , vol.735 , pp. 234-242
    • Gliozi, A.1    Paoli, G.2    De Rosa, M.3    Gambbacorta, A.4
  • 22
    • 0031744571 scopus 로고    scopus 로고
    • Hyperthermophiles and the problem of DNA instability
    • Grogan D. W. (1998) Hyperthermophiles and the problem of DNA instability. Mol. Microbiol. 28: 1043-1049
    • (1998) Mol. Microbiol. , vol.28 , pp. 1043-1049
    • Grogan, D.W.1
  • 23
    • 0030900384 scopus 로고    scopus 로고
    • Relationships between genomic G+C content, RNA secundary structures and optimal growth temperature in prokaryotes
    • Galtier N. and Lobry J.R. (1997) Relationships between genomic G+C content, RNA secundary structures and optimal growth temperature in prokaryotes. J. Mol. Evol. 44: 632-636
    • (1997) J. Mol. Evol. , vol.44 , pp. 632-636
    • Galtier, N.1    Lobry, J.R.2
  • 24
    • 0036716945 scopus 로고    scopus 로고
    • Stability of mRNA in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Bini E., Dikshit V., Dirksen K., Drozda M. and Blum P. (2002) Stability of mRNA in the hyperthermophilic archaeon Sulfolobus solfataricus. RNA 8: 1129-1136
    • (2002) RNA , vol.8 , pp. 1129-1136
    • Bini, E.1    Dikshit, V.2    Dirksen, K.3    Drozda, M.4    Blum, P.5
  • 25
    • 0026766429 scopus 로고
    • Di-myo-inositol-1,1′-phosphate: A new inositol phosphate isolated from Pyrococcus woesei
    • Scholz S., Sonnenbichler J., Schafer W. and Hensel R. (1992) Di-myo-inositol-1,1′-phosphate: a new inositol phosphate isolated from Pyrococcus woesei. FEBS Lett. 306: 239-242
    • (1992) FEBS Lett. , vol.306 , pp. 239-242
    • Scholz, S.1    Sonnenbichler, J.2    Schafer, W.3    Hensel, R.4
  • 26
    • 0001912876 scopus 로고
    • Thermoadaptation of methanogenic bacteria by intracellular ion concentration
    • Hensel R. and König H. (1988) Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 49: 75-79
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 75-79
    • Hensel, R.1    König, H.2
  • 28
    • 20544443981 scopus 로고    scopus 로고
    • Stabilization of nucleic acids by unusual polyamines produced by an extreme thermophile, Thermus thermophilus
    • Terui Y., Ohnuma M., Hiraga K., Kawashima F. and Oshima, T. (2005) Stabilization of nucleic acids by unusual polyamines produced by an extreme thermophile, Thermus thermophilus. Biochem. J. 388: 427-433
    • (2005) Biochem. J. , vol.388 , pp. 427-433
    • Terui, Y.1    Ohnuma, M.2    Hiraga, K.3    Kawashima, F.4    Oshima, T.5
  • 30
    • 0029886852 scopus 로고    scopus 로고
    • The unique DNA topology and DNA topoisomerases of hyperthermophilic archaea
    • Forterre P., Bergerat A. and Lopez-Garcia P. (1996) The unique DNA topology and DNA topoisomerases of hyperthermophilic archaea. FEMS Microbiol. Rev. 18: 237-248
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 237-248
    • Forterre, P.1    Bergerat, A.2    Lopez-Garcia, P.3
  • 31
    • 0030931040 scopus 로고    scopus 로고
    • Both DNA gyrase and reverse gyrase are present in the hyperthermophilic bacterium Thermotoga maritima
    • USA
    • Guipaud O., Marguet E., Knoll K. M., Boutier de la Tour C. and Forterre P. (1997) Both DNA gyrase and reverse gyrase are present in the hyperthermophilic bacterium Thermotoga maritima. Proc. Natl. Acad. Sci. USA 94: 10606-10611
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 10606-10611
    • Guipaud, O.1    Marguet, E.2    Knoll, K.M.3    Boutier De La Tour, C.4    Forterre, P.5
  • 32
    • 0021017817 scopus 로고
    • Histone-like protein in the Archaebacterium Sulfolobus acidocaldarius
    • Green G. R., Searcy D. G. and DeLange R. J. (1983) Histone-like protein in the Archaebacterium Sulfolobus acidocaldarius. Biochim. Biophys. Acta 741: 251-257
    • (1983) Biochim. Biophys. Acta , vol.741 , pp. 251-257
    • Green, G.R.1    Searcy, D.G.2    Delange, R.J.3
  • 33
    • 0037009516 scopus 로고    scopus 로고
    • Structure of Alba: An archaeal chromatin protein modulated by acetylation
    • Wardleworth B. N., Russelt R. J. M., Bell S. D., Taylor G. L. and White M. F. (2002) Structure of Alba: an archaeal chromatin protein modulated by acetylation. EMBO J. 21: 4654-4662
    • (2002) EMBO J. , vol.21 , pp. 4654-4662
    • Wardleworth, B.N.1    Russelt, R.J.M.2    Bell, S.D.3    Taylor, G.L.4    White, M.F.5
  • 34
    • 0032144071 scopus 로고    scopus 로고
    • Histones and nucleosomes in Archaea and Eukarya: A comparative analysis
    • Pereira S. L. and Reeve J. N. (1998) Histones and nucleosomes in Archaea and Eukarya: a comparative analysis. Extremophiles 2: 141-148
    • (1998) Extremophiles , vol.2 , pp. 141-148
    • Pereira, S.L.1    Reeve, J.N.2
  • 35
    • 0029669996 scopus 로고    scopus 로고
    • Purification and characterization of a histone-like protein from the Archaeal isolate AN1, a member of the Thermococcales
    • Ronimus R. S. and Musgrave D. R. (1996) Purification and characterization of a histone-like protein from the Archaeal isolate AN1, a member of the Thermococcales. Mol. Microbiol. 20: 77-86
    • (1996) Mol. Microbiol. , vol.20 , pp. 77-86
    • Ronimus, R.S.1    Musgrave, D.R.2
  • 36
    • 0032815173 scopus 로고    scopus 로고
    • Control of DNA topology during thermal stress in hyperthermophilic archaea: DNA topoisomersase levels, activities and induced thermotolerance during heat and cold shock in Sulfolobus
    • Lopez-Garcia P. and Forterre P. (1999) Control of DNA topology during thermal stress in hyperthermophilic archaea: DNA topoisomersase levels, activities and induced thermotolerance during heat and cold shock in Sulfolobus. Mol. Microbiol. 33: 766-777
    • (1999) Mol. Microbiol. , vol.33 , pp. 766-777
    • Lopez-Garcia, P.1    Forterre, P.2
  • 37
    • 0032417610 scopus 로고    scopus 로고
    • Temperature, template topology and factor requirement of archaeal transcription
    • USA
    • Bell S. D., Jaxel C., Nadal M., Kosa P. F. and Jackson S. P. (1998) Temperature, template topology and factor requirement of archaeal transcription. Proc. Natl. Acad. Sci. USA 95: 15218-15222
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 15218-15222
    • Bell, S.D.1    Jaxel, C.2    Nadal, M.3    Kosa, P.F.4    Jackson, S.P.5
  • 38
    • 0030985997 scopus 로고    scopus 로고
    • Rates of spontaneous mutation in an archaeon from geothermal environments
    • Jacobs K. L. and Grogan D. W. (1997) Rates of spontaneous mutation in an archaeon from geothermal environments. J. Bacteriol. 179: 3298-3303
    • (1997) J. Bacteriol. , vol.179 , pp. 3298-3303
    • Jacobs, K.L.1    Grogan, D.W.2
  • 39
    • 0030272402 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase activities in thermophilic micro-organisms
    • Koulis A., Cowan D. A., Pearl L. H. and Savva R. (1996) Uracil-DNA glycosylase activities in thermophilic micro-organisms. FEMS Microbiol. Lett. 143: 267-271
    • (1996) FEMS Microbiol. Lett. , vol.143 , pp. 267-271
    • Koulis, A.1    Cowan, D.A.2    Pearl, L.H.3    Savva, R.4
  • 40
    • 0030928340 scopus 로고    scopus 로고
    • Photoreactivation in an archaeon from geothermal environments
    • Grogan D. W. (1997) Photoreactivation in an archaeon from geothermal environments. Microbiology 143: 1071-1076
    • (1997) Microbiology , vol.143 , pp. 1071-1076
    • Grogan, D.W.1
  • 41
    • 0030961061 scopus 로고    scopus 로고
    • Genetic responses of the thermophilic archaeon Sulfolobus acidocaldarius to short-wavelength UV light
    • Wood E. R., Ghane F. and Grogan, D. W. (1997) Genetic responses of the thermophilic archaeon Sulfolobus acidocaldarius to short-wavelength UV light. J. Bacteriol. 179: 5693-5698
    • (1997) J. Bacteriol. , vol.179 , pp. 5693-5698
    • Wood, E.R.1    Ghane, F.2    Grogan, D.W.3
  • 42
    • 0037079680 scopus 로고    scopus 로고
    • A DNA repair system specific for thermophilic Archaea and bacteria predicted by genomic context analysis
    • Makarova K. S., Aravind L., Grishin N. V., Rogozin I. B. and Koonin E. V. (2002) A DNA repair system specific for thermophilic Archaea and bacteria predicted by genomic context analysis. Nucleic Acids Res. 30: 482-496
    • (2002) Nucleic Acids Res. , vol.30 , pp. 482-496
    • Makarova, K.S.1    Aravind, L.2    Grishin, N.V.3    Rogozin, I.B.4    Koonin, E.V.5
  • 43
    • 0030856630 scopus 로고    scopus 로고
    • Cell cycle characteristics of thermophilic archaea
    • Bemander R and Poplawski A. (1997) Cell cycle characteristics of thermophilic archaea. J. Bacteriol. 179: 4963-4969
    • (1997) J. Bacteriol. , vol.179 , pp. 4963-4969
    • Bemander, R.1    Poplawski, A.2
  • 44
    • 0018116757 scopus 로고
    • An enhanced thermostability in thermophilic 5-S ribonucleic acids under physiological salt conditions
    • Nazar R. N., Sprott G. D., Matheson A. T. and Van N. T. (1978) An enhanced thermostability in thermophilic 5-S ribonucleic acids under physiological salt conditions. Biochim. Biophys. Acta 521: 288-294
    • (1978) Biochim. Biophys. Acta , vol.521 , pp. 288-294
    • Nazar, R.N.1    Sprott, G.D.2    Matheson, A.T.3    Van, N.T.4
  • 45
    • 0036606141 scopus 로고    scopus 로고
    • Evidence for strong selective constraint acting on the nucleotide composition of 16S ribosomal RNA genes
    • Wang H. C. and Hickey D. A. (2002) Evidence for strong selective constraint acting on the nucleotide composition of 16S ribosomal RNA genes. Nucleic Acids Res. 30: 2501-2507
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2501-2507
    • Wang, H.C.1    Hickey, D.A.2
  • 46
    • 0032528883 scopus 로고    scopus 로고
    • Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA
    • Kohrer C., Mayer C., Neumair O., Grobner P. and Piendl W. (1998) Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA. Eur. J. Biochem. 256: 97-105
    • (1998) Eur. J. Biochem. , vol.256 , pp. 97-105
    • Kohrer, C.1    Mayer, C.2    Neumair, O.3    Grobner, P.4    Piendl, W.5
  • 47
    • 0035912931 scopus 로고    scopus 로고
    • Recognition of 16S rRNA by ribosomal protein S4 from Bacillus stearothermophilus
    • Gerstner R. B., Pak Y. and Draper D. E. (2001) Recognition of 16S rRNA by ribosomal protein S4 from Bacillus stearothermophilus. Biochemistry 40: 7165-7173
    • (2001) Biochemistry , vol.40 , pp. 7165-7173
    • Gerstner, R.B.1    Pak, Y.2    Draper, D.E.3
  • 48
    • 0035407085 scopus 로고    scopus 로고
    • Study of the binding of the S7 protein with 16S rRNA fragment 926-986/1219-1393 as a key step in the assembly of the small subunit of prokaryotic ribosomes
    • Mosk.
    • Rassokhin T. I., Golovin A. V., Petrova E. B., Spiridonova V. A., Karginova O. A., Rozhdestvenskii T. S. et al. (2001) Study of the binding of the S7 protein with 16S rRNA fragment 926-986/1219-1393 as a key step in the assembly of the small subunit of prokaryotic ribosomes. Mol. Biol. (Mosk.) 35: 617-627
    • (2001) Mol. Biol. , vol.35 , pp. 617-627
    • Rassokhin, T.I.1    Golovin, A.V.2    Petrova, E.B.3    Spiridonova, V.A.4    Karginova, O.A.5    Rozhdestvenskii, T.S.6
  • 49
    • 0042063940 scopus 로고    scopus 로고
    • Affinity of ribosomal protein S8 from mesophilic and (hyper)thermophilic archaea and bacteria for 16S rRNA correlates with the growth temperatures of the organisms
    • Gruber T., Kohrer C., Lung B., Shcherbakov D. and Piendl W. (2003) Affinity of ribosomal protein S8 from mesophilic and (hyper)thermophilic archaea and bacteria for 16S rRNA correlates with the growth temperatures of the organisms. FEBS Lett. 549: 123-128
    • (2003) FEBS Lett. , vol.549 , pp. 123-128
    • Gruber, T.1    Kohrer, C.2    Lung, B.3    Shcherbakov, D.4    Piendl, W.5
  • 50
    • 0032455220 scopus 로고    scopus 로고
    • Posttranscriptional modifications in 16S and 23S rRNAs of the archaeal hyperthermophile Sulfolobus solfataricus
    • Noon K. R., Bruenger E. and McCloskey J. A. (1998) Posttranscriptional modifications in 16S and 23S rRNAs of the archaeal hyperthermophile Sulfolobus solfataricus. J. Bacteriol. 180: 2883-2888
    • (1998) J. Bacteriol. , vol.180 , pp. 2883-2888
    • Noon, K.R.1    Bruenger, E.2    McCloskey, J.A.3
  • 52
    • 0002090634 scopus 로고    scopus 로고
    • Modified nucleosides in translation
    • Grosjean H. and Benne R. (eds.), ASM Press, Washington, DC
    • Curran J. F. (1998) Modified nucleosides in translation. In: Modification and Editing of RNA, pp. 493-516, Grosjean H. and Benne R. (eds.), ASM Press, Washington, DC
    • (1998) Modification and Editing of RNA , pp. 493-516
    • Curran, J.F.1
  • 53
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giegé R., Sissler M. and Florentz C. (1998) Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res. 26: 5017-5035
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5017-5035
    • Giegé, R.1    Sissler, M.2    Florentz, C.3
  • 54
    • 0015541340 scopus 로고
    • The effect of growth temperatures on the in vivo ribose methylation of Bacillus stearothermophilus transfer RNA
    • Agris P. F., Koh H. and Soll D. (1973) The effect of growth temperatures on the in vivo ribose methylation of Bacillus stearothermophilus transfer RNA. Arch. Biochem. Biophys. 154: 277-282
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 277-282
    • Agris, P.F.1    Koh, H.2    Soll, D.3
  • 55
    • 0017173794 scopus 로고
    • Heat-induced stability of tRNA from an extreme thermophile, Thermus thermophilus
    • Watanabe K., Shinma M., Oshima T. and Nishimura S. (1976) Heat-induced stability of tRNA from an extreme thermophile, Thermus thermophilus. Biochem. Biophys. Res. Commun. 72: 1137-1144
    • (1976) Biochem. Biophys. Res. Commun. , vol.72 , pp. 1137-1144
    • Watanabe, K.1    Shinma, M.2    Oshima, T.3    Nishimura, S.4
  • 56
    • 0022273096 scopus 로고
    • 1 species from an extreme thermophile, Thermus thermophilus HB8: Effect of 2-thiolation of ribothymidine on the thermostability of tRNA
    • 1 species from an extreme thermophile, Thermus thermophilus HB8: effect of 2-thiolation of ribothymidine on the thermostability of tRNA. Biochemistry 24: 5711-5715
    • (1985) Biochemistry , vol.24 , pp. 5711-5715
    • Horie, N.1    Hara-Yokoyama, M.2    Yokoyama, S.3    Watanabe, K.4    Kuchino, Y.5    Nishimura, S.6
  • 57
    • 0018832937 scopus 로고
    • Thermally induced biosynthesis of 2′-O-methylguanosine in tRNA from an extreme thermophile, Thermus thermophilus HB27
    • USA
    • Kumagai I., Watanabe K. and Oshima T. (1980) Thermally induced biosynthesis of 2′-O-methylguanosine in tRNA from an extreme thermophile, Thermus thermophilus HB27. Proc. Natl. Acad. Sci. USA 77: 1922-1926
    • (1980) Proc. Natl. Acad. Sci. , vol.77 , pp. 1922-1926
    • Kumagai, I.1    Watanabe, K.2    Oshima, T.3
  • 59
    • 0035890653 scopus 로고    scopus 로고
    • Post-transcriptional modification in archaeal tRNAs: Identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic Methanococcales
    • McCloskey J. A., Graham D. E., Zhou S., Grain P. F., Ibba M., Konisky J. et al. (2001) Post-transcriptional modification in archaeal tRNAs: identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic Methanococcales. Nucleic Acids Res. 29: 4699-4706
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4699-4706
    • McCloskey, J.A.1    Graham, D.E.2    Zhou, S.3    Grain, P.F.4    Ibba, M.5    Konisky, J.6
  • 60
    • 0026524798 scopus 로고
    • Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2′-hydroxyl group
    • Kawai G., Yamamoto Y., Kamimura T., Masegi T., Sekine M., Hata T. et al. (1992) Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2′-hydroxyl group. Biochemistry 31: 1040-1046
    • (1992) Biochemistry , vol.31 , pp. 1040-1046
    • Kawai, G.1    Yamamoto, Y.2    Kamimura, T.3    Masegi, T.4    Sekine, M.5    Hata, T.6
  • 61
    • 0015503195 scopus 로고
    • Relation between aminoacyl-tRNA stability and the fixed amino acid
    • Hentzen D., Mandel P. and Garel J. P. (1972) Relation between aminoacyl-tRNA stability and the fixed amino acid. Biochim. Biophys. Acta 281: 228-232
    • (1972) Biochim. Biophys. Acta , vol.281 , pp. 228-232
    • Hentzen, D.1    Mandel, P.2    Garel, J.P.3
  • 62
    • 0034991910 scopus 로고    scopus 로고
    • The renaissance of aminoacyl-tRNA synthesis
    • Ibba M. and Söll D. (2001) The renaissance of aminoacyl-tRNA synthesis. EMBO Rep. 2: 382-387
    • (2001) EMBO Rep. , vol.2 , pp. 382-387
    • Ibba, M.1    Söll, D.2
  • 63
    • 0013122119 scopus 로고    scopus 로고
    • Thermal stability of aminoacyl-tRNAs in aqueous solutions
    • Stepanov V. G. and Nyborg J. (2002) Thermal stability of aminoacyl-tRNAs in aqueous solutions. Extremophiles 6: 485-490
    • (2002) Extremophiles , vol.6 , pp. 485-490
    • Stepanov, V.G.1    Nyborg, J.2
  • 64
    • 0034855858 scopus 로고    scopus 로고
    • How do thermophilic proteins deal with heat?
    • Kumar S. and Nussinov R. (2001) How do thermophilic proteins deal with heat? Cell. Mol. Life Sci. 58: 1216-1223
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1216-1223
    • Kumar, S.1    Nussinov, R.2
  • 65
    • 0033616712 scopus 로고    scopus 로고
    • Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species
    • USA
    • Haney P. J., Badger J. H., Buldak G. L., Reich C. I., Woese C. R. and Olsen G. J. (1999) Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species. Proc. Natl. Acad. Sci. USA 96: 3578-3583
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 3578-3583
    • Haney, P.J.1    Badger, J.H.2    Buldak, G.L.3    Reich, C.I.4    Woese, C.R.5    Olsen, G.J.6
  • 66
    • 0036742110 scopus 로고    scopus 로고
    • Compatible solutes of organisms that live in hot saline environments
    • Santos H. and da Costa M. S. (2002) Compatible solutes of organisms that live in hot saline environments. Environ. Microbiol. 4: 501-509
    • (2002) Environ. Microbiol. , vol.4 , pp. 501-509
    • Santos, H.1    Da Costa, M.S.2
  • 67
    • 0034636987 scopus 로고    scopus 로고
    • The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds
    • Toth E. A., Worby C., Dixon J. E., Goedken E. R., Marqusee S. and Yeates T. O. (2000) The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. J. Mol. Biol. 301: 433-450
    • (2000) J. Mol. Biol. , vol.301 , pp. 433-450
    • Toth, E.A.1    Worby, C.2    Dixon, J.E.3    Goedken, E.R.4    Marqusee, S.5    Yeates, T.O.6
  • 68
    • 0037022796 scopus 로고    scopus 로고
    • A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond
    • Meyer J., Clay M. D., Johnson M. K., Stubna A., Munck E., Higgins C. et al. (2002) A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond. Biochemistry 41: 3096-3108
    • (2002) Biochemistry , vol.41 , pp. 3096-3108
    • Meyer, J.1    Clay, M.D.2    Johnson, M.K.3    Stubna, A.4    Munck, E.5    Higgins, C.6
  • 70
    • 0035155348 scopus 로고    scopus 로고
    • Experimental evolution of enzyme temperature profile: Selection in vivo and characterization of low-temperature-adapted mutants of Pyrococcus furiosus ornithine carbamoyltransferase
    • Roovers M., Sanchez R., Legrain C. and Glansdorff N. (2001) Experimental evolution of enzyme temperature profile: selection in vivo and characterization of low-temperature-adapted mutants of Pyrococcus furiosus ornithine carbamoyltransferase. J. Bacteriol. 183: 1101-1105
    • (2001) J. Bacteriol. , vol.183 , pp. 1101-1105
    • Roovers, M.1    Sanchez, R.2    Legrain, C.3    Glansdorff, N.4
  • 71
    • 0031935580 scopus 로고    scopus 로고
    • Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
    • Akanuma S., Yamagishi A., Tanaka N. and Oshima T. (1998) Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. Protein Sci. 7: 698-705
    • (1998) Protein Sci. , vol.7 , pp. 698-705
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 72
    • 0029019280 scopus 로고
    • Did primitive microorganisms use non-haem iron proteins in place of NAD/P?
    • Daniel R. M. and Danson M. J. (1995) Did primitive microorganisms use non-haem iron proteins in place of NAD/P? J. Mol. Evol. 40: 559-560
    • (1995) J. Mol. Evol. , vol.40 , pp. 559-560
    • Daniel, R.M.1    Danson, M.J.2
  • 73
    • 0028049261 scopus 로고
    • Pyruvate ferredoxin oxidoreductases of the hyperthermophilic archaeon Pyrococcus furiosus and the hyperthermophilic bacterium Thermotoga maritima have different catalytic mechanisms
    • Smith E. T., Blamey J. M. and Adams M. W. W. (1994) Pyruvate ferredoxin oxidoreductases of the hyperthermophilic archaeon Pyrococcus furiosus and the hyperthermophilic bacterium Thermotoga maritima have different catalytic mechanisms. Biochemistry 33: 1008-1016
    • (1994) Biochemistry , vol.33 , pp. 1008-1016
    • Smith, E.T.1    Blamey, J.M.2    Adams, M.W.W.3
  • 74
    • 2342568994 scopus 로고    scopus 로고
    • Metabolic channeling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus: Dynamic enzyme-enzyme interactions involved in the formation of the channeling complex
    • Massant J. and Glansdorff N. (2004) Metabolic channeling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus: dynamic enzyme-enzyme interactions involved in the formation of the channeling complex. Biochem. Soc. Trans. 32: 306-309
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 306-309
    • Massant, J.1    Glansdorff, N.2
  • 76
    • 29344465133 scopus 로고    scopus 로고
    • Carbamate kinase interacts with ornithine carbamoyltransferase and aspartate carbamoyl-transferase to channel carbamoyl phosphate in arginine and pyrimidine biosynthesis in Pyrococcus furiosus
    • Massant J. and Glansdorff N. (2005) Carbamate kinase interacts with ornithine carbamoyltransferase and aspartate carbamoyl-transferase to channel carbamoyl phosphate in arginine and pyrimidine biosynthesis in Pyrococcus furiosus. Archaea 1: 365-373
    • (2005) Archaea , vol.1 , pp. 365-373
    • Massant, J.1    Glansdorff, N.2
  • 77
    • 0030957783 scopus 로고    scopus 로고
    • Structure of carbamoyl phosphate synthetase: A journey of 96Å from substrate to product
    • Thoden J. B., Holden H. M., Wesenberg G., Raushel F. M. and Rayment I. (1997) Structure of carbamoyl phosphate synthetase: a journey of 96Å from substrate to product. Biochemistry 36: 6305-6316
    • (1997) Biochemistry , vol.36 , pp. 6305-6316
    • Thoden, J.B.1    Holden, H.M.2    Wesenberg, G.3    Raushel, F.M.4    Rayment, I.5
  • 78
    • 0032729457 scopus 로고    scopus 로고
    • Carbamoyl phosphate synthetase: An amazing biochemical odyssey from substrate to product
    • Holden H. M., Thoden J. B. and Raushel F. M. (1999) Carbamoyl phosphate synthetase: an amazing biochemical odyssey from substrate to product. Cell. Mol. Life Sci. 56: 507-522
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 507-522
    • Holden, H.M.1    Thoden, J.B.2    Raushel, F.M.3
  • 79
    • 10644271631 scopus 로고    scopus 로고
    • Archaeal genetics, the third way
    • Allers T. and Mevarech M. (2005) Archaeal genetics, the third way. Nat. Rev. Genet. 6: 58-73
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 58-73
    • Allers, T.1    Mevarech, M.2
  • 81
    • 2342544133 scopus 로고    scopus 로고
    • Exceptionally diverse morphotypes and genomes of crenarchaeal hyperthermophilic viruses
    • Prangishvilli D. and Garrett R. A. (2004) Exceptionally diverse morphotypes and genomes of crenarchaeal hyperthermophilic viruses. Biochem. Soc. Trans. 32: 204-208
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 204-208
    • Prangishvilli, D.1    Garrett, R.A.2
  • 82
    • 0029895213 scopus 로고    scopus 로고
    • Exchange of genetic markers at extremely high temperatures in the archaeon Sulfolobus acidocaldarius. I
    • Grogan D. W. (1996) Exchange of genetic markers at extremely high temperatures in the archaeon Sulfolobus acidocaldarius. I. Bacteriol. 178: 3207-3211
    • (1996) Bacteriol. , vol.178 , pp. 3207-3211
    • Grogan, D.W.1
  • 83
    • 8744225606 scopus 로고    scopus 로고
    • Genomic comparison of archaeal conjugative plasmids from Sulfolobus
    • Greve B., Jensen S., Brügger K., Zillig W. and Garrett R. A. (2004) Genomic comparison of archaeal conjugative plasmids from Sulfolobus. Archaea 1: 231-239
    • (2004) Archaea , vol.1 , pp. 231-239
    • Greve, B.1    Jensen, S.2    Brügger, K.3    Zillig, W.4    Garrett, R.A.5
  • 84
    • 0036840170 scopus 로고    scopus 로고
    • Construction of a shuttle vector for, and spheroplast transformation of, the hyperthermophilic archaeon Pyrococcus abyssi
    • Lucas S., Toffin L., Zivanovic Y., Charlier D., Moussard H., Forterre P. et al. (2002) Construction of a shuttle vector for, and spheroplast transformation of, the hyperthermophilic archaeon Pyrococcus abyssi. Appl. Environ. Microbiol. 68: 5528-5536
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5528-5536
    • Lucas, S.1    Toffin, L.2    Zivanovic, Y.3    Charlier, D.4    Moussard, H.5    Forterre, P.6
  • 85
    • 0038460077 scopus 로고    scopus 로고
    • A reporter gene system for the hyperthermophilic archaeon Sulfolobus solfataricus based on a selectable and integrative shuttle vector
    • Jonuscheit M., Martusewitsch E., Stedman K. M. and Schleper C. (2003) A reporter gene system for the hyperthermophilic archaeon Sulfolobus solfataricus based on a selectable and integrative shuttle vector. Mol. Microbiol. 48: 1241-1252
    • (2003) Mol. Microbiol. , vol.48 , pp. 1241-1252
    • Jonuscheit, M.1    Martusewitsch, E.2    Stedman, K.M.3    Schleper, C.4
  • 86
    • 0037494948 scopus 로고    scopus 로고
    • Characterization and functional complementation of non-lethal deletion in the chromosome of a β-glycosidase mutant of Sulfolobus solfataricus
    • Bartolucci S., Rossi M. and Cannio R. (2003) Characterization and functional complementation of non-lethal deletion in the chromosome of a β-glycosidase mutant of Sulfolobus solfataricus. J. Bacteriol. 185: 3948-3957
    • (2003) J. Bacteriol. , vol.185 , pp. 3948-3957
    • Bartolucci, S.1    Rossi, M.2    Cannio, R.3
  • 87
    • 4644342125 scopus 로고    scopus 로고
    • The role of cis-acting sequences governing catabolite repression control of lacS expression in the archaeon Sulfolobus solfataricus
    • Hoang V., Bini E., Dixit V., Drozda M. and Blum P. (2004) The role of cis-acting sequences governing catabolite repression control of lacS expression in the archaeon Sulfolobus solfataricus. Genetics 167: 1563-1572
    • (2004) Genetics , vol.167 , pp. 1563-1572
    • Hoang, V.1    Bini, E.2    Dixit, V.3    Drozda, M.4    Blum, P.5
  • 88
    • 0347285395 scopus 로고    scopus 로고
    • Occurrence and characterization of mercury resistance in the hyperthermophilic archaeon Sulfolobus solfataricus by use of gene disruption
    • Schelert J., Dixit V., Hoang V., Simbahan J., Drozda M. and Blum P. (2004) Occurrence and characterization of mercury resistance in the hyperthermophilic archaeon Sulfolobus solfataricus by use of gene disruption. J. Bacteriol. 186: 427-437
    • (2004) J. Bacteriol. , vol.186 , pp. 427-437
    • Schelert, J.1    Dixit, V.2    Hoang, V.3    Simbahan, J.4    Drozda, M.5    Blum, P.6
  • 89
    • 0027957161 scopus 로고
    • Quorum sensing in bacteria: The LuxR-LuxI family of cell density-responsive transcriptional regulators
    • Fuqua W. C., Winans S. C. and Greenberg, E. P. (1994) Quorum sensing in bacteria: the LuxR-LuxI family of cell density-responsive transcriptional regulators. J. Bacteriol. 176: 269-275
    • (1994) J. Bacteriol. , vol.176 , pp. 269-275
    • Fuqua, W.C.1    Winans, S.C.2    Greenberg, E.P.3
  • 90
    • 0037123780 scopus 로고    scopus 로고
    • Small talk. Cell-to-cell communication in bacteria
    • Bassler B. L. (2002) Small talk. Cell-to-cell communication in bacteria. Cell 109: 421-424
    • (2002) Cell , vol.109 , pp. 421-424
    • Bassler, B.L.1
  • 91
    • 3142764130 scopus 로고    scopus 로고
    • Cell-to cell signalling in Escherichia coli and Salmonella enterica
    • Ahmer B. M. M. (2004) Cell-to cell signalling in Escherichia coli and Salmonella enterica. Mol. Microbiol. 52: 933-945
    • (2004) Mol. Microbiol. , vol.52 , pp. 933-945
    • Ahmer, B.M.M.1
  • 92
    • 0842306822 scopus 로고    scopus 로고
    • Cell density-dependent regulation: Basic principles and effects on the virulence of Gram-positive cocci
    • Podbielski A. and Kreikemeyer B. (2004) Cell density-dependent regulation: basic principles and effects on the virulence of Gram-positive cocci. Int. J. Infect. Dis. 8: 81-95
    • (2004) Int. J. Infect. Dis. , vol.8 , pp. 81-95
    • Podbielski, A.1    Kreikemeyer, B.2
  • 93
    • 8144228289 scopus 로고    scopus 로고
    • Transcriptional analysis of biofilm formation processes in the anaerobic, hyperthermophilic bacterium Thermotoga maritima
    • Pysz M. A., Conners S. B., Montera C. I., Shockley K. R., Johnson M. R., Ward D. E. et al. (2004) Transcriptional analysis of biofilm formation processes in the anaerobic, hyperthermophilic bacterium Thermotoga maritima. Appl. Environ. Microbiol. 70: 6098-6112
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6098-6112
    • Pysz, M.A.1    Conners, S.B.2    Montera, C.I.3    Shockley, K.R.4    Johnson, M.R.5    Ward, D.E.6
  • 94
    • 13444272004 scopus 로고    scopus 로고
    • Population density-dependent regulation of exopolysaccharide formation in the hyperthermophilic bacterium Thermotoga maritima
    • Johnson M. R., Montera C. I., Conners S. B., Shockley K. R., Bridger S.L. and Kelly R. M. (2005) Population density-dependent regulation of exopolysaccharide formation in the hyperthermophilic bacterium Thermotoga maritima. Mol. Microbiol. 55: 664-674
    • (2005) Mol. Microbiol. , vol.55 , pp. 664-674
    • Johnson, M.R.1    Montera, C.I.2    Conners, S.B.3    Shockley, K.R.4    Bridger, S.L.5    Kelly, R.M.6


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