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Volumn 15, Issue 3, 2005, Pages 352-363

Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; METAL ION; NUCLEOTIDE; PYRUVIC ACID; SULFUR; AMINO ACID; ARCHAEAL PROTEIN;

EID: 13544250517     PISSN: 10889051     EISSN: None     Source Type: Journal    
DOI: 10.1101/gr.3003105     Document Type: Article
Times cited : (370)

References (82)
  • 1
    • 0035158352 scopus 로고    scopus 로고
    • Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
    • Adams, M.W., Holden, J.F., Menon, A.L., Schut, G.J., Grunden, A.M., Hou, C., Hutchins, A.M., Jenney Jr., F.E., Kim, C., Ma, K., et al. 2001. Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183: 716-724.
    • (2001) J. Bacteriol. , vol.183 , pp. 716-724
    • Adams, M.W.1    Holden, J.F.2    Menon, A.L.3    Schut, G.J.4    Grunden, A.M.5    Hou, C.6    Hutchins, A.M.7    Jenney Jr., F.E.8    Kim, C.9    Ma, K.10
  • 3
    • 0035093350 scopus 로고    scopus 로고
    • Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and Bacteria
    • Amend, J.P. and Shock, E.L. 2001. Energetics of overall metabolic reactions of thermophilic and hyperthermophilic Archaea and Bacteria. FEMS Microbiol. Rev. 25: 175-243.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 175-243
    • Amend, J.P.1    Shock, E.L.2
  • 4
    • 8444239349 scopus 로고    scopus 로고
    • Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1
    • Atomi, H., Fukui, T., Kanai, T., Morikawa, M., and Imanaka, T. 2004. Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1. Archaea 1: 263-267.
    • (2004) Archaea , vol.1 , pp. 263-267
    • Atomi, H.1    Fukui, T.2    Kanai, T.3    Morikawa, M.4    Imanaka, T.5
  • 5
    • 0032900737 scopus 로고    scopus 로고
    • CRITICA: Coding region identification tool invoking comparative analysis
    • Badger, J.H. and Olsen, G.J. 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
  • 6
    • 0034677790 scopus 로고    scopus 로고
    • Elucidation of determinants of protein stability through genome sequence analysis
    • Chakravarty, S. and Varadarajan, R. 2000. Elucidation of determinants of protein stability through genome sequence analysis. FEBS Lett. 470: 65-69.
    • (2000) FEBS Lett. , vol.470 , pp. 65-69
    • Chakravarty, S.1    Varadarajan, R.2
  • 7
    • 0034707197 scopus 로고    scopus 로고
    • Comparison between Pyrococcus horikoshii and Pyrococcus abyssi genome sequences reveals linkage of restriction-modification genes with large genome polymorphisms
    • Chinen, A., Uchiyama, I., and Kobayashi, I. 2000. Comparison between Pyrococcus horikoshii and Pyrococcus abyssi genome sequences reveals linkage of restriction-modification genes with large genome polymorphisms. Gene 259: 109-121.
    • (2000) Gene , vol.259 , pp. 109-121
    • Chinen, A.1    Uchiyama, I.2    Kobayashi, I.3
  • 10
    • 7744224800 scopus 로고    scopus 로고
    • Identification and functional verification of archaeal-type phosphoenolpyruvate carboxylase, a missing link in archaeal central carbohydrate metabolism
    • Ettema, T.J., Makarova, K.S., Jellema, G.L., Gierman, H.J., Koonin, E.V., Huynen, M.A., de Vos, W.M., and van der Oost, J. 2004. Identification and functional verification of archaeal-type phosphoenolpyruvate carboxylase, a missing link in archaeal central carbohydrate metabolism. J. Bacteriol. 186: 7754-7762.
    • (2004) J. Bacteriol. , vol.186 , pp. 7754-7762
    • Ettema, T.J.1    Makarova, K.S.2    Jellema, G.L.3    Gierman, H.J.4    Koonin, E.V.5    Huynen, M.A.6    de Vos, W.M.7    van der Oost, J.8
  • 11
    • 0033582465 scopus 로고    scopus 로고
    • Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1
    • Ezaki, S., Maeda, N., Kishimoto, T., Atomi, H., and Imanaka, T. 1999. Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1. J. Biol. Chem. 274: 5078-5082.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5078-5082
    • Ezaki, S.1    Maeda, N.2    Kishimoto, T.3    Atomi, H.4    Imanaka, T.5
  • 12
    • 3042775352 scopus 로고    scopus 로고
    • First characterization of an archaeal GTP-dependent phosphoenolpyruvate carboxykinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Fukuda, W., Fukui, T., Atomi, H., and Imanaka, T. 2004. First characterization of an archaeal GTP-dependent phosphoenolpyruvate carboxykinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 186: 4620-4627.
    • (2004) J. Bacteriol. , vol.186 , pp. 4620-4627
    • Fukuda, W.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 13
    • 0032857545 scopus 로고    scopus 로고
    • Cloning of an α-glucosidase gene from Thermococcus hydrothermalis by functional complementation of a Saccharomyces cerevisiae mal11 mutant strain
    • Galichet, A. and Belarbi, A. 1999. Cloning of an α-glucosidase gene from Thermococcus hydrothermalis by functional complementation of a Saccharomyces cerevisiae mal11 mutant strain. FEBS Lett. 458: 188-192.
    • (1999) FEBS Lett. , vol.458 , pp. 188-192
    • Galichet, A.1    Belarbi, A.2
  • 14
    • 1542682737 scopus 로고    scopus 로고
    • Archeal DNA replication: Eukaryal proteins in a bacterial context
    • Grabowski, B. and Kelman, Z. 2003. Archeal DNA replication: Eukaryal proteins in a bacterial context. Annu. Rev. Microbiol. 57: 487-516.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 487-516
    • Grabowski, B.1    Kelman, Z.2
  • 15
    • 0033616712 scopus 로고    scopus 로고
    • Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species
    • 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. 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
  • 16
    • 0034889240 scopus 로고    scopus 로고
    • Extracellular synthesis, specific recognition, and intracellular degradation of cyclomaltodextrins by the hyperthermophilic archaeon Thermococcus sp. strain B1001
    • Hashimoto, Y., Yamamoto, T., Fujiwara, S., Takagi, M., and Imanaka, T. 2001. Extracellular synthesis, specific recognition, and intracellular degradation of cyclomaltodextrins by the hyperthermophilic archaeon Thermococcus sp. strain B1001. J. Bacteriol. 183: 5050-5057.
    • (2001) J. Bacteriol. , vol.183 , pp. 5050-5057
    • Hashimoto, Y.1    Yamamoto, T.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 17
    • 0037507306 scopus 로고    scopus 로고
    • Helicase and nuclease activities of hyperthermophile Pyrococcus horikoshii Dna2 inhibited by substrates with RNA segments at 5′-end
    • Higashibata, H., Kikuchi, H., Kawarabayasi, Y., and Matsui, I. 2003. Helicase and nuclease activities of hyperthermophile Pyrococcus horikoshii Dna2 inhibited by substrates with RNA segments at 5′-end. J. Biol. Chem. 278: 15983-15990.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15983-15990
    • Higashibata, H.1    Kikuchi, H.2    Kawarabayasi, Y.3    Matsui, I.4
  • 18
    • 0035000622 scopus 로고    scopus 로고
    • Diversity among three novel groups of hyperthermophilic deep-sea Thermococcus species from three sites in the northeastern Pacific Ocean
    • Holden, J.F., Takai, K,, Summit, M., Bolton, S., Zyskowski, J., and Baross, J.A. 2001. Diversity among three novel groups of hyperthermophilic deep-sea Thermococcus species from three sites in the northeastern Pacific Ocean. FEMS Microbiol. Ecol. 36: 51-60.
    • (2001) FEMS Microbiol. Ecol. , vol.36 , pp. 51-60
    • Holden, J.F.1    Takai, K.2    Summit, M.3    Bolton, S.4    Zyskowski, J.5    Baross, J.A.6
  • 19
    • 0035141843 scopus 로고    scopus 로고
    • Discovery of hyperthermophilic microorganisms
    • Huber, R. and Stetter, K.O. 2001. Discovery of hyperthermophilic microorganisms. Methods Enzymol. 330: 11-24.
    • (2001) Methods Enzymol. , vol.330 , pp. 11-24
    • Huber, R.1    Stetter, K.O.2
  • 20
    • 0035171348 scopus 로고    scopus 로고
    • Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Hutchins, A.M., Holden, J.F., and Adams, M.W. 2001. Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183: 709-715.
    • (2001) J. Bacteriol. , vol.183 , pp. 709-715
    • Hutchins, A.M.1    Holden, J.F.2    Adams, M.W.3
  • 21
    • 0037067223 scopus 로고    scopus 로고
    • Expression of long- and short-type FK506 binding proteins in hyperthermophilic archaea
    • Ideno, A. and Maruyama, T. 2002. Expression of long- and short-type FK506 binding proteins in hyperthermophilic archaea. Gene 292: 57-63.
    • (2002) Gene , vol.292 , pp. 57-63
    • Ideno, A.1    Maruyama, T.2
  • 22
    • 0035878729 scopus 로고    scopus 로고
    • FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins
    • Ideno, A., Yoshida, T., Iida, T., Furutani, M., and Maruyama, T. 2001. FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins. Biochem. J. 357: 465-471.
    • (2001) Biochem. J. , vol.357 , pp. 465-471
    • Ideno, A.1    Yoshida, T.2    Iida, T.3    Furutani, M.4    Maruyama, T.5
  • 23
    • 0036356457 scopus 로고    scopus 로고
    • Catalyzing "hot" reactions: Enzymes from hyperthermophilic Archaea
    • Imanaka, T. and Atomi, H. 2002. Catalyzing "hot" reactions: Enzymes from hyperthermophilic Archaea. Chem. Rec. 2: 149-163.
    • (2002) Chem. Rec. , vol.2 , pp. 149-163
    • Imanaka, T.1    Atomi, H.2
  • 24
    • 0141957432 scopus 로고    scopus 로고
    • Taxonomy of nonmethanogenic hyperthermophilic and related thermophilic archaea
    • Itoh, T. 2003. Taxonomy of nonmethanogenic hyperthermophilic and related thermophilic archaea. J. Biosci. Bioeng. 96: 203-212.
    • (2003) J. Biosci. Bioeng. , vol.96 , pp. 203-212
    • Itoh, T.1
  • 25
    • 0032937393 scopus 로고    scopus 로고
    • Isolation and characterization of a second subunit of molecular chaperonin from Pyrococcus kodakaraensis KOD1: Analysis of an ATPase-deficient mutant enzyme
    • Izumi, M., Fujiwara, S., Takagi, M., Kanaya, S., and Imanaka, T. 1999. Isolation and characterization of a second subunit of molecular chaperonin from Pyrococcus kodakaraensis KOD1: Analysis of an ATPase-deficient mutant enzyme. Appl. Environ. Microbiol. 65: 1801-1805.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1801-1805
    • Izumi, M.1    Fujiwara, S.2    Takagi, M.3    Kanaya, S.4    Imanaka, T.5
  • 26
    • 0034812522 scopus 로고    scopus 로고
    • Two kinds of archaeal chaperonin with different temperature dependency from a hyperthermophile
    • Izumi, M., Fujiwara, S., Takagi, M., Fukui, K., and Imanaka, T. 2001. Two kinds of archaeal chaperonin with different temperature dependency from a hyperthermophile. Biochem. Biophys. Res. Commun. 280: 581-587.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 581-587
    • Izumi, M.1    Fujiwara, S.2    Takagi, M.3    Fukui, K.4    Imanaka, T.5
  • 27
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney Jr., F.E., Verhagen, M.F., Cui, X., and Adams, M.W. 1999. Anaerobic microbes: Oxygen detoxification without superoxide dismutase. Science 286: 306-309.
    • (1999) Science , vol.286 , pp. 306-309
    • Jenney Jr., F.E.1    Verhagen, M.F.2    Cui, X.3    Adams, M.W.4
  • 28
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B.T., and MacKinnon, R. 2002. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417: 515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 29
    • 0037369931 scopus 로고    scopus 로고
    • Characterization of a cytosolic NiFe-hydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Kanai, T., Ito, S., and Imanaka, T. 2003. Characterization of a cytosolic NiFe-hydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 185: 1705-1711.
    • (2003) J. Bacteriol. , vol.185 , pp. 1705-1711
    • Kanai, T.1    Ito, S.2    Imanaka, T.3
  • 32
    • 0034984584 scopus 로고    scopus 로고
    • Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry
    • Kitano, K., Maeda, N., Fukui, T., Atomi, H., Imanaka, T., and Miki, K. 2001. Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry. Structure (Camb) 9: 473-481.
    • (2001) Structure (Camb.) , vol.9 , pp. 473-481
    • Kitano, K.1    Maeda, N.2    Fukui, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 33
    • 0032989249 scopus 로고    scopus 로고
    • Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: Lysine is synthesized via α-aminoadipic acid not via diaminopimelic acid
    • Kobashi, N., Nishiyama, M., and Tanokura, M. 1999. Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: Lysine is synthesized via α-aminoadipic acid not via diaminopimelic acid. J. Bacteriol. 181: 1713-1718.
    • (1999) J. Bacteriol. , vol.181 , pp. 1713-1718
    • Kobashi, N.1    Nishiyama, M.2    Tanokura, M.3
  • 34
    • 0011731008 scopus 로고    scopus 로고
    • Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeon Pyrococcus furiosus
    • Koning, S.M., Konings, W.N., and Driessen, A.J.M. 2002. Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeon Pyrococcus furiosus. Archaea 1: 19-25.
    • (2002) Archaea , vol.1 , pp. 19-25
    • Koning, S.M.1    Konings, W.N.2    Driessen, A.J.M.3
  • 35
  • 36
    • 0030854739 scopus 로고    scopus 로고
    • tRNAscan-SE: A program for improved detection of transfer RNA genes in genomic sequence
    • Lowe, T.M. and Eddy, S.R. 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
  • 37
  • 38
    • 0034990899 scopus 로고    scopus 로고
    • Ferredoxin:NADP oxidoreductase from Pyrococcus furiosus
    • Ma, K. and Adams, M.W. 2001. Ferredoxin:NADP oxidoreductase from Pyrococcus furiosus. Methods Enzymol. 334: 40-45.
    • (2001) Methods Enzymol. , vol.334 , pp. 40-45
    • Ma, K.1    Adams, M.W.2
  • 39
    • 0034065733 scopus 로고    scopus 로고
    • Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction
    • Ma, K., Weiss, R., and Adams, M.W. 2000. Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. 182: 1864-1871.
    • (2000) J. Bacteriol. , vol.182 , pp. 1864-1871
    • Ma, K.1    Weiss, R.2    Adams, M.W.3
  • 40
    • 0033569351 scopus 로고    scopus 로고
    • Ribulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structure
    • Maeda, N., Kitano, K., Fukui, T., Ezaki, S., Atomi, H., Miki, K., and Imanaka, T. 1999. Ribulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structure. J. Mol. Biol. 293: 57-66.
    • (1999) J. Mol. Biol. , vol.293 , pp. 57-66
    • Maeda, N.1    Kitano, K.2    Fukui, T.3    Ezaki, S.4    Atomi, H.5    Miki, K.6    Imanaka, T.7
  • 43
    • 0345363243 scopus 로고    scopus 로고
    • Nucleoid structure and partition in Methanococcus jannaschii: An archaeon with multiple copies of the chromosome
    • Malandrin, L., Huber, H., and Bernander, R. 1999. Nucleoid structure and partition in Methanococcus jannaschii: An archaeon with multiple copies of the chromosome. Genetics 152: 1315-1323.
    • (1999) Genetics , vol.152 , pp. 1315-1323
    • Malandrin, L.1    Huber, H.2    Bernander, R.3
  • 44
    • 0034004192 scopus 로고    scopus 로고
    • High spontaneous mutation rate in the hyperthermophilic archaeon Sulfolobus solfataricus is mediated by transposable elements
    • Martusewitsch, E., Sensen, C.W., and Schleper, C. 2000. High spontaneous mutation rate in the hyperthermophilic archaeon Sulfolobus solfataricus is mediated by transposable elements. J. Bacteriol. 182: 2574-2581.
    • (2000) J. Bacteriol. , vol.182 , pp. 2574-2581
    • Martusewitsch, E.1    Sensen, C.W.2    Schleper, C.3
  • 45
    • 0032737311 scopus 로고    scopus 로고
    • Patterns of temperature adaptation in proteins from Methanococcus and Bacillus
    • McDonald, J.H., Grasso, A.M., and Rejto, L.K. 1999. Patterns of temperature adaptation in proteins from Methanococcus and Bacillus. Mol. Biol. Evol. 16: 1785-1790.
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 1785-1790
    • McDonald, J.H.1    Grasso, A.M.2    Rejto, L.K.3
  • 46
    • 0036790007 scopus 로고    scopus 로고
    • Microbial genome evolution: Sources of variability
    • Mira, A., Klasson, L., and Andersson, S.G. 2002. Microbial genome evolution: Sources of variability. Curr. Opin. Microbiol. 5: 506-512.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 506-512
    • Mira, A.1    Klasson, L.2    Andersson, S.G.3
  • 47
    • 0033552649 scopus 로고    scopus 로고
    • Proportion of membrane proteins in proteomes of 15 single-cell organisms analyzed by the SOSUI prediction system
    • Mitaku, S., Ono, M., Hirokawa, T., Boon-Chieng, S., and Sonoyama, M. 1999. Proportion of membrane proteins in proteomes of 15 single-cell organisms analyzed by the SOSUI prediction system. Biophys. Chem. 82: 165-171.
    • (1999) Biophys. Chem. , vol.82 , pp. 165-171
    • Mitaku, S.1    Ono, M.2    Hirokawa, T.3    Boon-Chieng, S.4    Sonoyama, M.5
  • 48
    • 0027946790 scopus 로고
    • Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp
    • Morikawa, M., Izawa, Y., Rashid, N., Hoaki, T., and Imanaka, T. 1994. Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp. Appl. Environ. Microbiol. 60: 4559-4566.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4559-4566
    • Morikawa, M.1    Izawa, Y.2    Rashid, N.3    Hoaki, T.4    Imanaka, T.5
  • 51
    • 0037025191 scopus 로고    scopus 로고
    • An alternative flavin-dependent mechanism for thymidylate synthesis
    • Myllykallio, H., Lipowski, G., Leduc, D., Filee, J., Forterre, P., and Liebl, U. 2002. An alternative flavin-dependent mechanism for thymidylate synthesis. Science 297: 105-107.
    • (2002) Science , vol.297 , pp. 105-107
    • Myllykallio, H.1    Lipowski, G.2    Leduc, D.3    Filee, J.4    Forterre, P.5    Liebl, U.6
  • 52
    • 0034666611 scopus 로고    scopus 로고
    • Cloning, expression and biochemical characterisation of a unique thermostable pullulan-hydrolysing enzyme from the hyperthermophilic archaeon Thermococcus aggregans
    • Niehaus, F., Peters, A., Groudieva, T., and Antranikian, G. 2000. Cloning, expression and biochemical characterisation of a unique thermostable pullulan-hydrolysing enzyme from the hyperthermophilic archaeon Thermococcus aggregans. FEMS Microbiol. Lett. 190: 223-229.
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 223-229
    • Niehaus, F.1    Peters, A.2    Groudieva, T.3    Antranikian, G.4
  • 53
    • 0037810546 scopus 로고    scopus 로고
    • Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens
    • Nishio, Y., Nakamura, Y., Kawarabayasi, Y., Usuda, Y., Kimura, E., Sugimoto, S., Matsui, K., Yamagishi, A., Kikuchi, H., Ikeo, K., et al. 2003. Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens. Genome Res. 13: 1572-1579.
    • (2003) Genome Res. , vol.13 , pp. 1572-1579
    • Nishio, Y.1    Nakamura, Y.2    Kawarabayasi, Y.3    Usuda, Y.4    Kimura, E.5    Sugimoto, S.6    Matsui, K.7    Yamagishi, A.8    Kikuchi, H.9    Ikeo, K.10
  • 55
    • 0034682335 scopus 로고    scopus 로고
    • Lateral gene transfer and the nature of bacterial innovation
    • Ochman, H., Lawrence, J.G., and Groisman, E.A. 2000. Lateral gene transfer and the nature of bacterial innovation. Nature 405: 299-304.
    • (2000) Nature , vol.405 , pp. 299-304
    • Ochman, H.1    Lawrence, J.G.2    Groisman, E.A.3
  • 56
    • 0033952662 scopus 로고    scopus 로고
    • Culture-dependent and culture-independent characterization of microbial assemblages associated with high-temperature petroleum reservoirs
    • Orphan, V.J., Taylor, L.T., Hafenbradl, D., and Delong, E.F. 2000. Culture-dependent and culture-independent characterization of microbial assemblages associated with high-temperature petroleum reservoirs. Appl. Environ. Microbiol. 66: 700-711.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 700-711
    • Orphan, V.J.1    Taylor, L.T.2    Hafenbradl, D.3    Delong, E.F.4
  • 57
    • 0034602365 scopus 로고    scopus 로고
    • Evolution of the family of pRN plasmids and their integrase-mediated insertion into the chromosome of the crenarchaeon Sulfolobus solfataricus
    • Peng, X., Holz, I., Zillig, W., Garrett, R.A,, and She, Q. 2000. Evolution of the family of pRN plasmids and their integrase-mediated insertion into the chromosome of the crenarchaeon Sulfolobus solfataricus. J. Mol. Biol. 303: 449-454.
    • (2000) J. Mol. Biol. , vol.303 , pp. 449-454
    • Peng, X.1    Holz, I.2    Zillig, W.3    Garrett, R.A.4    She, Q.5
  • 58
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The Intein database
    • Perler, F.B. 2002. InBase: The Intein database. Nucleic Acids Res. 30: 383-384.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 59
    • 0036181524 scopus 로고    scopus 로고
    • Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain
    • Rashid, N., Cornista, J., Ezaki, S., Fukui, T., Atomi, H., and Imanaka, T. 2002a. Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain. J. Bacteriol. 184: 777-784.
    • (2002) J. Bacteriol. , vol.184 , pp. 777-784
    • Rashid, N.1    Cornista, J.2    Ezaki, S.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 60
    • 0037163028 scopus 로고    scopus 로고
    • A novel candidate for the true fructose-1,6-bisphosphatase in archaea
    • Rashid, N., Imanaka, H., Kanai, T., Fukui, T., Atomi, H., and Imanaka, T. 2002b. A novel candidate for the true fructose-1,6-bisphosphatase in archaea. J. Biol. Chem. 277: 30649-30655.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30649-30655
    • Rashid, N.1    Imanaka, H.2    Kanai, T.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 61
    • 3042565616 scopus 로고    scopus 로고
    • Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate aldolase reveals a metabolic link between pentoses and central carbon metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis
    • Rashid, N., Imanaka, H., Fukui, T., Atomi, H., and Imanaka, T. 2004. Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate aldolase reveals a metabolic link between pentoses and central carbon metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis. J. Bacteriol. 186: 4185-4191.
    • (2004) J. Bacteriol. , vol.186 , pp. 4185-4191
    • Rashid, N.1    Imanaka, H.2    Fukui, T.3    Atomi, H.4    Imanaka, T.5
  • 64
    • 0036082038 scopus 로고    scopus 로고
    • Novel energy metabolism in anaerobic hyperthermophilic archaea: A modified Embden-Meyerhof pathway
    • Sakuraba, H. and Ohshima, T. 2002. Novel energy metabolism in anaerobic hyperthermophilic archaea: A modified Embden-Meyerhof pathway. J. Biosci. Bioeng. 93: 441-448.
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 441-448
    • Sakuraba, H.1    Ohshima, T.2
  • 65
    • 0037934657 scopus 로고    scopus 로고
    • A simple energy-conserving system: Proton reduction coupled to proton translocation
    • Sapra, R., Bagramyan, K., and Adams, M.W. 2003. A simple energy-conserving system: Proton reduction coupled to proton translocation. Proc. Natl. Acad. Sci. 100: 7545-7550.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 7545-7550
    • Sapra, R.1    Bagramyan, K.2    Adams, M.W.3
  • 66
    • 0037215528 scopus 로고    scopus 로고
    • Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Sato, T., Fukui, T., Atomi, H., and Imanaka, T. 2003. Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 185: 210-220.
    • (2003) J. Bacteriol. , vol.185 , pp. 210-220
    • Sato, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 67
    • 4344692495 scopus 로고    scopus 로고
    • Genetic evidence identifying the true gluconeogenic fructose-1,6-bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles
    • Sato, T., Imanaka, H., Rashid, N., Fukui, T., Atomi, H., and Imanaka, T. 2004. Genetic evidence identifying the true gluconeogenic fructose-1,6-bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles. J. Bacteriol. 186: 5799-5807.
    • (2004) J. Bacteriol. , vol.186 , pp. 5799-5807
    • Sato, T.1    Imanaka, H.2    Rashid, N.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 68
    • 0035945570 scopus 로고    scopus 로고
    • Gene capture in archaeal chromosomes
    • She, Q., Peng, X., Zillig, W., and Garrett, R.A. 2001. Gene capture in archaeal chromosomes. Nature 409: 478.
    • (2001) Nature , vol.409 , pp. 478
    • She, Q.1    Peng, X.2    Zillig, W.3    Garrett, R.A.4
  • 69
    • 0033756225 scopus 로고    scopus 로고
    • MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase
    • Stec, B., Yang, H., Johnson, K.A., Chen, L., and Roberts, M.F. 2000. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat. Struct. Biol. 7: 1046-1050.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1046-1050
    • Stec, B.1    Yang, H.2    Johnson, K.A.3    Chen, L.4    Roberts, M.F.5
  • 70
    • 0029859281 scopus 로고    scopus 로고
    • Cloning and expression of the α-amylase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme
    • Tachibana, Y., Leclere, M.M., Fujiwara, S., Takagi, M., and Imanaka, T. 1996. Cloning and expression of the α-amylase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme. J. Ferment. Bioeng. 82: 224-232.
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 224-232
    • Tachibana, Y.1    Leclere, M.M.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 71
    • 0030808181 scopus 로고    scopus 로고
    • Cloning and expression of the 4-α-glucanotransferase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme
    • Tachibana, Y., Fujiwara, S., Takagi, M., and Imanaka, T. 1997. Cloning and expression of the 4-α-glucanotransferase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme. J. Ferment. Bioeng. 83: 540-548.
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 540-548
    • Tachibana, Y.1    Fujiwara, S.2    Takagi, M.3    Imanaka, T.4
  • 72
    • 0032728411 scopus 로고    scopus 로고
    • A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1
    • Tanaka, T., Fujiwara, S., Nishikori, S., Fukui, T., Takagi, M., and Imanaka, T. 1999. A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1. Appl. Environ. Microbiol. 65: 5338-5344.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5338-5344
    • Tanaka, T.1    Fujiwara, S.2    Nishikori, S.3    Fukui, T.4    Takagi, M.5    Imanaka, T.6
  • 73
    • 0035929579 scopus 로고    scopus 로고
    • Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Tanaka, T., Fukui, T., and Imanaka, T. 2001. Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 276: 35629-35635.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35629-35635
    • Tanaka, T.1    Fukui, T.2    Imanaka, T.3
  • 74
    • 0042890412 scopus 로고    scopus 로고
    • Characterization of an exo-β-D-glucosaminidase involved in a novel chitinolytic pathway from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Tanaka, T., Fukui, T., Atomi, H., and Imanaka, T. 2003. Characterization of an exo-β-D-glucosaminidase involved in a novel chitinolytic pathway from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 185: 5175-5181.
    • (2003) J. Bacteriol. , vol.185 , pp. 5175-5181
    • Tanaka, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 75
    • 3142721163 scopus 로고    scopus 로고
    • Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Tanaka, T., Fukui, T., Fujiwara, S., Atomi, H., and Imanaka, T. 2004. Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 279: 30021-30027.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30021-30027
    • Tanaka, T.1    Fukui, T.2    Fujiwara, S.3    Atomi, H.4    Imanaka, T.5
  • 77
    • 0032561335 scopus 로고    scopus 로고
    • The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation
    • van der Oost, J., Schut, G., Kengen, S.W., Hagen, W.R., Thomm, M., and de Vos, W.M. 1998. The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation. J. Biol. Chem. 273: 28149-28154.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28149-28154
    • van der Oost, J.1    Schut, G.2    Kengen, S.W.3    Hagen, W.R.4    Thomm, M.5    de Vos, W.M.6
  • 78
    • 0028929082 scopus 로고
    • Minimal amino-acid-requirements of the hyperthermophilic archaeon Pyrococcus abyssi, isolated from deep-sea hydrothermal vents
    • Watrin, L., Martinjezequel, V., and Prieur, D. 1995. Minimal amino-acid-requirements of the hyperthermophilic archaeon Pyrococcus abyssi, isolated from deep-sea hydrothermal vents. Appl. Environ. Microbiol. 61: 1138-1140.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1138-1140
    • Watrin, L.1    Martinjezequel, V.2    Prieur, D.3
  • 79
    • 1542723403 scopus 로고    scopus 로고
    • CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea
    • Woodson, J.D. and Escalante-Semerena, J.C. 2004. CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea. Proc. Natl. Acad. Sci. 101: 3591-3596.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 3591-3596
    • Woodson, J.D.1    Escalante-Semerena, J.C.2
  • 80
    • 0345529065 scopus 로고    scopus 로고
    • A new pathway for salvaging the coenzyme B12 precursor cobinamide in archaea requires cobinamide-phosphate synthase (CbiB) enzyme activity
    • Woodson, J.D., Zayas, C.L., and Escalante-Semerena, J.C. 2003. A new pathway for salvaging the coenzyme B12 precursor cobinamide in archaea requires cobinamide-phosphate synthase (CbiB) enzyme activity. J. Bacteriol. 185: 7193-7201.
    • (2003) J. Bacteriol. , vol.185 , pp. 7193-7201
    • Woodson, J.D.1    Zayas, C.L.2    Escalante-Semerena, J.C.3
  • 81
    • 0035973555 scopus 로고    scopus 로고
    • A novel bacterial gene-finding system with improved accuracy in locating start codons
    • Yada, T., Totoki, Y., Takagi, T., and Nakai, K. 2001. A novel bacterial gene-finding system with improved accuracy in locating start codons. DNA Res. 8: 97-106.
    • (2001) DNA Res. , vol.8 , pp. 97-106
    • Yada, T.1    Totoki, Y.2    Takagi, T.3    Nakai, K.4
  • 82
    • 0036567231 scopus 로고    scopus 로고
    • Pyrococcus genome comparison evidences chromosome shuffling-driven evolution
    • Zivanovic, Y., Lopez, P., Philippe, H., and Forterre, P. 2002. Pyrococcus genome comparison evidences chromosome shuffling-driven evolution. Nucleic Acids Res. 30: 1902-1910.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1902-1910
    • Zivanovic, Y.1    Lopez, P.2    Philippe, H.3    Forterre, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.