메뉴 건너뛰기




Volumn 3, Issue 2, 2012, Pages

Engineering a hyperthermophilic archaeon for temperature dependent product formation

Author keywords

[No Author keywords available]

Indexed keywords

BIOFUEL; ACETIC ACID DERIVATIVE; BACTERIAL PROTEIN; HYDROGEN; LACTATE DEHYDROGENASE; LACTIC ACID;

EID: 84860522983     PISSN: None     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00053-12     Document Type: Article
Times cited : (48)

References (29)
  • 1
    • 33749835755 scopus 로고    scopus 로고
    • History of discovery of the first hyperthermophiles
    • Stetter KO. 2006. History of discovery of the first hyperthermophiles. Extremophiles 10:357-362.
    • (2006) Extremophiles , vol.10 , pp. 357-362
    • Stetter, K.O.1
  • 4
    • 80053385099 scopus 로고    scopus 로고
    • Application of hyperthermophiles and their enzymes
    • Atomi H, Sato T, Kanai T. 2011. Application of hyperthermophiles and their enzymes. Curr. Opin. Biotechnol. 22:618-626.
    • (2011) Curr. Opin. Biotechnol , vol.22 , pp. 618-626
    • Atomi, H.1    Sato, T.2    Kanai, T.3
  • 5
    • 0347285395 scopus 로고    scopus 로고
    • Occurrence and characterization of mercury resistance in the hyperthermophilic archaeon Sulfolobus solfataricus by use of gene disruption
    • Schelert J, et al. 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
  • 6
    • 59749097200 scopus 로고    scopus 로고
    • Expanding and understanding the genetic toolbox of the hyperthermophilic genus Sulfolobus
    • Wagner M, et al. 2009. Expanding and understanding the genetic toolbox of the hyperthermophilic genus Sulfolobus. Biochem. Soc. Trans. 37: 97-101.
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 97-101
    • Wagner, M.1
  • 7
    • 0037215528 scopus 로고    scopus 로고
    • Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Sato T, Fukui T, Atomi H, 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
  • 8
    • 79953288906 scopus 로고    scopus 로고
    • Natural competence in the hyperthermophilic archaeon Pyrococcus furiosus facilitates genetic manipulation: Construction of markerless deletions of genes encoding the two cytoplasmic hydrogenases
    • Lipscomb GL, et al. 2011. Natural competence in the hyperthermophilic archaeon Pyrococcus furiosus facilitates genetic manipulation: construction of markerless deletions of genes encoding the two cytoplasmic hydrogenases. Appl. Environ. Microbiol. 77:2232-2238.
    • (2011) Appl. Environ. Microbiol , vol.77 , pp. 2232-2238
    • Lipscomb, G.L.1
  • 9
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
    • Fiala G, Stetter KO. 1986. Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C. Arch. Microbiol. 145:56-61.
    • (1986) Arch. Microbiol , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 10
    • 57049181957 scopus 로고    scopus 로고
    • Hydrogenesis in hyperthermophilic microorganisms: Implications for biofuels
    • Chou CJ, Jenney FE, Adams MW, Kelly RM. 2008. Hydrogenesis in hyperthermophilic microorganisms: implications for biofuels. Metab. Eng. 10:394-404.
    • (2008) Metab. Eng , vol.10 , pp. 394-404
    • Chou, C.J.1    Jenney, F.E.2    Adams, M.W.3    Kelly, R.M.4
  • 11
    • 80055032687 scopus 로고    scopus 로고
    • Homologous expression of a subcomplex of Pyrococcus furiosus hydrogenase that interacts with pyruvate ferredoxin oxidoreductase
    • Hopkins RC, et al. 2011. Homologous expression of a subcomplex of Pyrococcus furiosus hydrogenase that interacts with pyruvate ferredoxin oxidoreductase. PLoS One 6:e26569.
    • (2011) PLoS One , vol.6 , pp. 26569
    • Hopkins, R.C.1
  • 12
    • 76649127737 scopus 로고    scopus 로고
    • Thermococcus kodakarensis genetics: TK1827-encoded beta-glycosidase, new positive-selection protocol, and targeted and repetitive deletion technology
    • Santangelo TJ, Cubonová L, Reeve JN. 2010. Thermococcus kodakarensis genetics: TK1827-encoded beta-glycosidase, new positive-selection protocol, and targeted and repetitive deletion technology. Appl. Environ. Mi-crobiol. 76:1044-1052.
    • (2010) Appl. Environ. Mi-crobiol , vol.76 , pp. 1044-1052
    • Santangelo, T.J.1    Cubonová, L.2    Reeve, J.N.3
  • 13
    • 50949127622 scopus 로고    scopus 로고
    • Agmatine is essential for the cell growth of Thermococcus kodakaraensis
    • Fukuda W, Morimoto N, Imanaka T, Fujiwara S. 2008. Agmatine is essential for the cell growth of Thermococcus kodakaraensis. FEMS Microbiol. Lett. 287:113-120.
    • (2008) FEMS Microbiol. Lett , vol.287 , pp. 113-120
    • Fukuda, W.1    Morimoto, N.2    Imanaka, T.3    Fujiwara, S.4
  • 14
    • 77949820848 scopus 로고    scopus 로고
    • Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea
    • Ikeuchi Y, et al. 2010. Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea. Nat. Chem. Biol. 6:277-282.
    • (2010) Nat. Chem. Biol , vol.6 , pp. 277-282
    • Ikeuchi, Y.1
  • 15
    • 11144251737 scopus 로고    scopus 로고
    • Cold shock of a hyperthermophilic archaeon: Pyrococcus furiosus exhibits mul-tiple responses to a suboptimal growth temperature with a key role for membrane-bound glycoproteins
    • Weinberg MV, Schut GJ, Brehm S, Datta S, Adams MW. 2005. Cold shock of a hyperthermophilic archaeon: Pyrococcus furiosus exhibits mul-tiple responses to a suboptimal growth temperature with a key role for membrane-bound glycoproteins. J. Bacteriol. 187:336-348.
    • (2005) J. Bacteriol , vol.187 , pp. 336-348
    • Weinberg, M.V.1    Schut, G.J.2    Brehm, S.3    Datta, S.4    Adams, M.W.5
  • 16
    • 34147158720 scopus 로고    scopus 로고
    • Disruption of a sugar transporter gene cluster in a hyperthermophilic archaeon using a host-marker system based on antibiotic resistance
    • Matsumi R, Manabe K, Fukui T, Atomi H, Imanaka T. 2007. Disruption of a sugar transporter gene cluster in a hyperthermophilic archaeon using a host-marker system based on antibiotic resistance. J. Bacteriol. 189: 2683-2691.
    • (2007) J. Bacteriol , vol.189 , pp. 2683-2691
    • Matsumi, R.1    Manabe, K.2    Fukui, T.3    Atomi, H.4    Imanaka, T.5
  • 18
    • 67650457345 scopus 로고    scopus 로고
    • Efficient degradation of lignocellulosic plant biomass, without pretreatment, by the thermophilic anaerobe "Anaerocellum thermophilum" DSM 6725
    • Yang SJ, et al. 2009. Efficient degradation of lignocellulosic plant biomass, without pretreatment, by the thermophilic anaerobe "Anaerocellum thermophilum" DSM 6725. Appl. Environ. Microbiol. 75:4762-4769.
    • (2009) Appl. Environ. Microbiol , vol.75 , pp. 4762-4769
    • Yang, S.J.1
  • 19
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow near and above 100°C
    • Adams MW. 1993. Enzymes and proteins from organisms that grow near and above 100°C. Annu. Rev. Microbiol. 47:627-658.
    • (1993) Annu. Rev. Microbiol , vol.47 , pp. 627-658
    • Adams, M.W.1
  • 20
    • 0029923296 scopus 로고    scopus 로고
    • Extremely thermostable L()-lactate dehydrogenase from Thermotoga maritima: Cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state
    • Ostendorp R, Auerbach G, Jaenicke R. 1996. Extremely thermostable L()-lactate dehydrogenase from Thermotoga maritima: cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state. Protein. Sci. 5:862-873.
    • (1996) Protein. Sci , vol.5 , pp. 862-873
    • Ostendorp, R.1    Auerbach, G.2    Jaenicke, R.3
  • 21
    • 18844362113 scopus 로고    scopus 로고
    • Strategies for efficient production of heterologous proteins in Escherichia coli
    • Jana S, Deb JK. 2005. Strategies for efficient production of heterologous proteins in Escherichia coli. Appl. Microbiol. Biotechnol. 67:289-298.
    • (2005) Appl. Microbiol. Biotechnol , vol.67 , pp. 289-298
    • Jana, S.1    Deb, J.K.2
  • 22
    • 77951671134 scopus 로고    scopus 로고
    • Molecular genetic characterization of the thermostable L-lactate dehydrogenase gene (ldhL) of Thermoanaerobacter ethanolicus JW200 and biochemical characterization of the enzyme
    • Zhou Q, Shao WL. 2010. Molecular genetic characterization of the thermostable L-lactate dehydrogenase gene (ldhL) of Thermoanaerobacter ethanolicus JW200 and biochemical characterization of the enzyme. Bio-chemistry (Mosc) 75:526-530.
    • (2010) Bio-chemistry (Mosc) , vol.75 , pp. 526-530
    • Zhou, Q.1    Shao, W.L.2
  • 23
    • 79952152589 scopus 로고    scopus 로고
    • An engineered methanogenic pathway derived from the domains Bacteria and Archaea
    • Lessner DJ, Lhu L, Wahal CS, Ferry JG. 2010. An engineered methanogenic pathway derived from the domains Bacteria and Archaea. mBio 1:e00243-10.
    • (2010) MBio , vol.1
    • Lessner, D.J.1    Lhu, L.2    Wahal, C.S.3    Ferry, J.G.4
  • 24
    • 82755197372 scopus 로고    scopus 로고
    • Evolution of D-lactate dehydrogenase activity from glycerol dehydrogenase and its utility for D-lactate production from lignocellulose
    • Wang QZ, Ingram LO, Shanmugam KT. 2011. Evolution of D-lactate dehydrogenase activity from glycerol dehydrogenase and its utility for D-lactate production from lignocellulose. Proc. Natl. Acad. Sci. U. S. A. 108:18920-18925.
    • (2011) Proc. Natl. Acad. Sci. U. S. A , vol.108 , pp. 18920-18925
    • Wang, Q.Z.1    Ingram, L.O.2    Shanmugam, K.T.3
  • 25
    • 77956685960 scopus 로고    scopus 로고
    • Classification of "Anaerocellum thermophilum" strain DSM 6725 as Caldicellulosiruptor bescii sp. nov
    • Yang SJ, et al. 2010. Classification of "Anaerocellum thermophilum" strain DSM 6725 as Caldicellulosiruptor bescii sp. nov. Int. J. Syst. Evol. Microbiol. 60:2011-2015.
    • (2010) Int. J. Syst. Evol. Microbiol , vol.60 , pp. 2011-2015
    • Yang, S.J.1
  • 26
    • 0029031784 scopus 로고
    • Phylogenetic analyses of a new group of denitrifiers capable of anaerobic growth of toluene and description of Azoarcus tolulyticus sp. nov
    • Zhou JZ, Fries MR, Cheesanford JC, Tiedje JM. 1995. Phylogenetic analyses of a new group of denitrifiers capable of anaerobic growth of toluene and description of Azoarcus tolulyticus sp. nov. Int. J. Syst. Bacte-riol. 45:500-506.
    • (1995) Int. J. Syst. Bacte-riol , vol.45 , pp. 500-506
    • Zhou, J.Z.1    Fries, M.R.2    Cheesanford, J.C.3    Tiedje, J.M.4
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0037494947 scopus 로고    scopus 로고
    • Whole-genome DNA microarray analysis of a hyperthermophile and an archaeon: Pyrococcus furiosus grown on carbohydrates or peptides
    • Schut GJ, Brehm SD, Datta S, Adams MW. 2003. Whole-genome DNA microarray analysis of a hyperthermophile and an archaeon: Pyrococcus furiosus grown on carbohydrates or peptides. J. Bacteriol. 185:3935-3947.
    • (2003) J. Bacteriol , vol.185 , pp. 3935-3947
    • Schut, G.J.1    Brehm, S.D.2    Datta, S.3    Adams, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.