메뉴 건너뛰기




Volumn 74, Issue 10, 2011, Pages 1926-1933

Proteome analysis of thermococcus onnurineus NA1 reveals the expression of hydrogen gene cluster under carboxydotrophic growth

Author keywords

Carboxydotrophic growth; SDS PAGE LC MS MS; Thermococcus onnurineus NA1

Indexed keywords

CARBON MONOXIDE; HEAT SHOCK COGNATE PROTEIN 70; HYDROGENASE; METAGLIDASEN; PROTEOME;

EID: 80052025184     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.05.010     Document Type: Article
Times cited : (13)

References (39)
  • 1
    • 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., Baross J.A. Diversity among three novel groups of hyperthermophilic deep-sea Thermococcus species from three sites in the northeastern Pacific Ocean. FEMS Microbiol Ecol 2001, 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
  • 2
    • 33845593742 scopus 로고    scopus 로고
    • Thermoccoccus onnurineus sp. nov., a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent area at the PACMANUS field
    • Bae S.S., Kim Y.J., Yang S.H., Lim J.K., Jeon J.H., Lee H.S., et al. Thermoccoccus onnurineus sp. nov., a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent area at the PACMANUS field. J Microbiol Biotechnol 2006, 16:1826-1831.
    • (2006) J Microbiol Biotechnol , vol.16 , pp. 1826-1831
    • Bae, S.S.1    Kim, Y.J.2    Yang, S.H.3    Lim, J.K.4    Jeon, J.H.5    Lee, H.S.6
  • 3
    • 55549124188 scopus 로고    scopus 로고
    • The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism
    • Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., et al. The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism. J Bacteriol 2008, 190:7491-7499.
    • (2008) J Bacteriol , vol.190 , pp. 7491-7499
    • Lee, H.S.1    Kang, S.G.2    Bae, S.S.3    Lim, J.K.4    Cho, Y.5    Kim, Y.J.6
  • 4
    • 13544250517 scopus 로고    scopus 로고
    • Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes
    • Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T. Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res 2005, 15:352-363.
    • (2005) Genome Res , vol.15 , pp. 352-363
    • Fukui, T.1    Atomi, H.2    Kanai, T.3    Matsumi, R.4    Fujiwara, S.5    Imanaka, T.6
  • 5
    • 67650763466 scopus 로고    scopus 로고
    • Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea
    • Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M., et al. Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea. Genome Biol 2009, 10:R70.
    • (2009) Genome Biol , vol.10
    • Zivanovic, Y.1    Armengaud, J.2    Lagorce, A.3    Leplat, C.4    Guerin, P.5    Dutertre, M.6
  • 6
    • 9744254931 scopus 로고    scopus 로고
    • The first evidence of anaerobic CO oxidation coupled with H2 production by a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
    • Sokolova T.G., Jeanthon C., Kostrikina N.A., Chernyh N.A., Lebedinsky A.V., Stackebrandt E., et al. The first evidence of anaerobic CO oxidation coupled with H2 production by a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. Extremophiles 2004, 8:317-323.
    • (2004) Extremophiles , vol.8 , pp. 317-323
    • Sokolova, T.G.1    Jeanthon, C.2    Kostrikina, N.A.3    Chernyh, N.A.4    Lebedinsky, A.V.5    Stackebrandt, E.6
  • 7
    • 77956803428 scopus 로고    scopus 로고
    • Identification of a novel class of membrane-bound [NiFe]-hydrogenases in Thermococcus onnurineus NA1 by in silico analysis
    • Lim J.K., Kang S.G., Lebedinsky A.V., Lee J.H., Lee H.S. Identification of a novel class of membrane-bound [NiFe]-hydrogenases in Thermococcus onnurineus NA1 by in silico analysis. Appl Environ Microbiol 2010, 76:6286-6289.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 6286-6289
    • Lim, J.K.1    Kang, S.G.2    Lebedinsky, A.V.3    Lee, J.H.4    Lee, H.S.5
  • 8
  • 9
    • 61449182093 scopus 로고    scopus 로고
    • Proteomic characterization of the sulfur-reducing hyperthermophilic archaeon Thermococcus onnurineus NA1 by 2-DE/MS-MS
    • Kwon S.O., Kang S.G., Park S.H., Kim Y.H., Choi J.S., Lee J.H., et al. Proteomic characterization of the sulfur-reducing hyperthermophilic archaeon Thermococcus onnurineus NA1 by 2-DE/MS-MS. Extremophiles 2009, 13:379-387.
    • (2009) Extremophiles , vol.13 , pp. 379-387
    • Kwon, S.O.1    Kang, S.G.2    Park, S.H.3    Kim, Y.H.4    Choi, J.S.5    Lee, J.H.6
  • 10
    • 0003625509 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, F.T. Robb, A.R. Place, K.R. Sowers, H.J. Schreier, S. DasSarma, E.M. Fleischmann (Eds.)
    • Archaea: a laboratory manual 1995, Cold Spring Harbor Laboratory, Cold Spring Harbor. F.T. Robb, A.R. Place, K.R. Sowers, H.J. Schreier, S. DasSarma, E.M. Fleischmann (Eds.).
    • (1995) Archaea: a laboratory manual
  • 11
    • 0037640006 scopus 로고    scopus 로고
    • Thermococcus gammatolerans sp. nov., a hyperthermophilic archaeon from a deep-sea hydrothermal vent that resists ionizing radiation
    • Jolivet E., L'Haridon S., Corre E., Forterre P., Prieur D. Thermococcus gammatolerans sp. nov., a hyperthermophilic archaeon from a deep-sea hydrothermal vent that resists ionizing radiation. Int J Syst Evol Microbiol 2003, 53:847-851.
    • (2003) Int J Syst Evol Microbiol , vol.53 , pp. 847-851
    • Jolivet, E.1    L'Haridon, S.2    Corre, E.3    Forterre, P.4    Prieur, D.5
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0942265390 scopus 로고    scopus 로고
    • An analysis of the proteomic profile for Thermoanaerobacter tengcongensis under optimal culture conditions
    • Wang J., Xue Y., Feng X., Li X., Wang H., Li W., et al. An analysis of the proteomic profile for Thermoanaerobacter tengcongensis under optimal culture conditions. Proteomics 2004, 4:136-150.
    • (2004) Proteomics , vol.4 , pp. 136-150
    • Wang, J.1    Xue, Y.2    Feng, X.3    Li, X.4    Wang, H.5    Li, W.6
  • 14
    • 23944470397 scopus 로고    scopus 로고
    • Utility of electrophoretically derived protein mass estimates as additional constraints in proteome analysis of human serum based on MS/MS analysis
    • Kim J.Y., Lee J.H., Park G.W., Cho K., Kwon K.H., Park Y.M., et al. Utility of electrophoretically derived protein mass estimates as additional constraints in proteome analysis of human serum based on MS/MS analysis. Proteomics 2005, 5:3376-3385.
    • (2005) Proteomics , vol.5 , pp. 3376-3385
    • Kim, J.Y.1    Lee, J.H.2    Park, G.W.3    Cho, K.4    Kwon, K.H.5    Park, Y.M.6
  • 15
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • Kall L., Canterbury J.D., Weston J., Noble W.S., MacCoss M.J. Semi-supervised learning for peptide identification from shotgun proteomics datasets. Nat Methods 2007, 4:923-925.
    • (2007) Nat Methods , vol.4 , pp. 923-925
    • Kall, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    MacCoss, M.J.5
  • 16
    • 67049118923 scopus 로고    scopus 로고
    • Accurate and sensitive peptide identification with Mascot Percolator
    • Brosch M., Yu L., Hubbard T., Choudhary J. Accurate and sensitive peptide identification with Mascot Percolator. J Proteome Res 2009, 8:3176-3181.
    • (2009) J Proteome Res , vol.8 , pp. 3176-3181
    • Brosch, M.1    Yu, L.2    Hubbard, T.3    Choudhary, J.4
  • 17
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y., Oda Y., Tabata T., Sato T., Nagasu T., Rappsilber J., et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 2005, 4:1265-1272.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6
  • 19
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., Yates J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 20
    • 68549136910 scopus 로고    scopus 로고
    • Proteomics of Pyrococcus furiosus, a hyperthermophilic archaeon refractory to traditional methods
    • Lee A.M., Sevinsky J.R., Bundy J.L., Grunden A.M., Stephenson J.L. Proteomics of Pyrococcus furiosus, a hyperthermophilic archaeon refractory to traditional methods. J Proteome Res 2009, 8:3844-3851.
    • (2009) J Proteome Res , vol.8 , pp. 3844-3851
    • Lee, A.M.1    Sevinsky, J.R.2    Bundy, J.L.3    Grunden, A.M.4    Stephenson, J.L.5
  • 22
    • 49849095152 scopus 로고    scopus 로고
    • Identification and characterization of Sulfolobus solfataricus P2 proteome using multidimensional liquid phase protein separations
    • Assiddiq B.F., Snijders A.P., Chong P.K., Wright P.C., Dickman M.J. Identification and characterization of Sulfolobus solfataricus P2 proteome using multidimensional liquid phase protein separations. J Proteome Res 2008, 7:2253-2261.
    • (2008) J Proteome Res , vol.7 , pp. 2253-2261
    • Assiddiq, B.F.1    Snijders, A.P.2    Chong, P.K.3    Wright, P.C.4    Dickman, M.J.5
  • 23
    • 0028673449 scopus 로고
    • Characterization of three proteins containing multiple iron sites: rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster
    • Moura I., Tavares P., Ravi N. Characterization of three proteins containing multiple iron sites: rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster. Methods Enzymol 1994, 243:216-240.
    • (1994) Methods Enzymol , vol.243 , pp. 216-240
    • Moura, I.1    Tavares, P.2    Ravi, N.3
  • 24
    • 0035119328 scopus 로고    scopus 로고
    • Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high-molecular-weight rubredoxin
    • Das A., Coulter E.D., Kurtz D.M., Ljungdahl L.G. Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high-molecular-weight rubredoxin. J Bacteriol 2001, 183:1560-1567.
    • (2001) J Bacteriol , vol.183 , pp. 1560-1567
    • Das, A.1    Coulter, E.D.2    Kurtz, D.M.3    Ljungdahl, L.G.4
  • 25
    • 0036229440 scopus 로고    scopus 로고
    • Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis
    • Sztukowska M., Bugno M., Potempa J., Travis J., Kurtz D.M. Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis. Mol Microbiol 2002, 44:479-488.
    • (2002) Mol Microbiol , vol.44 , pp. 479-488
    • Sztukowska, M.1    Bugno, M.2    Potempa, J.3    Travis, J.4    Kurtz, D.M.5
  • 26
    • 9244263012 scopus 로고    scopus 로고
    • Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase
    • Weinberg M.V., Jenney F.E., Cui X., Adams M.W. Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase. J Bacteriol 2004, 186:7888-7895.
    • (2004) J Bacteriol , vol.186 , pp. 7888-7895
    • Weinberg, M.V.1    Jenney, F.E.2    Cui, X.3    Adams, M.W.4
  • 27
    • 62849119070 scopus 로고    scopus 로고
    • Ser/Thr/Tyr protein phosphorylation in the archaeon Halobacterium salinarum-a representative of the third domain of life
    • Aivaliotis M., Macek B., Gnad F., Reichelt P., Mann M., Oesterhelt D. Ser/Thr/Tyr protein phosphorylation in the archaeon Halobacterium salinarum-a representative of the third domain of life. PLoS One 2009, 4:e4777.
    • (2009) PLoS One , vol.4
    • Aivaliotis, M.1    Macek, B.2    Gnad, F.3    Reichelt, P.4    Mann, M.5    Oesterhelt, D.6
  • 29
    • 33745444345 scopus 로고    scopus 로고
    • The ribulose monophosphate pathway substitutes for the missing pentose phosphate pathway in the archaeon Thermococcus kodakaraensis
    • Orita I., Sato T., Yurimoto H., Kato N., Atomi H., Imanaka T., et al. The ribulose monophosphate pathway substitutes for the missing pentose phosphate pathway in the archaeon Thermococcus kodakaraensis. J Bacteriol 2006, 188:4698-4704.
    • (2006) J Bacteriol , vol.188 , pp. 4698-4704
    • Orita, I.1    Sato, T.2    Yurimoto, H.3    Kato, N.4    Atomi, H.5    Imanaka, T.6
  • 30
    • 0036837983 scopus 로고    scopus 로고
    • The first archaeal ATP-dependent glucokinase, from the hyperthermophilic crenarchaeon Aeropyrum pernix, represents a monomeric, extremely thermophilic ROK glucokinase with broad hexose specificity
    • Hansen T., Reichstein B., Schmid R., Schonheit P. The first archaeal ATP-dependent glucokinase, from the hyperthermophilic crenarchaeon Aeropyrum pernix, represents a monomeric, extremely thermophilic ROK glucokinase with broad hexose specificity. J Bacteriol 2002, 184:5955-5965.
    • (2002) J Bacteriol , vol.184 , pp. 5955-5965
    • Hansen, T.1    Reichstein, B.2    Schmid, R.3    Schonheit, P.4
  • 31
    • 20144364025 scopus 로고    scopus 로고
    • Biosynthesis of ribose-5-phosphate and erythrose-4-phosphate in Archaea: a phylogenetic analysis of archaeal genomes
    • Soderberg T. Biosynthesis of ribose-5-phosphate and erythrose-4-phosphate in Archaea: a phylogenetic analysis of archaeal genomes. Archaea 2005, 1:347-352.
    • (2005) Archaea , vol.1 , pp. 347-352
    • Soderberg, T.1
  • 32
    • 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., Imanaka T. First characterization of an archaeal GTP-dependent phosphoenolpyruvate carboxykinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Bacteriol 2004, 186:4620-4627.
    • (2004) J Bacteriol , vol.186 , pp. 4620-4627
    • Fukuda, W.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 33
    • 33847157932 scopus 로고    scopus 로고
    • Archaeal type III RuBisCOs function in a pathway for AMP metabolism
    • Sato T., Atomi H., Imanaka T. Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 2007, 315:1003-1006.
    • (2007) Science , vol.315 , pp. 1003-1006
    • Sato, T.1    Atomi, H.2    Imanaka, T.3
  • 34
    • 35148896749 scopus 로고    scopus 로고
    • Engineering of a type III RubisCO from a hyperthermophilic archaeon in order to enhance catalytic performance in mesophilic host cells
    • Yoshida S., Atomi H., Imanaka T. Engineering of a type III RubisCO from a hyperthermophilic archaeon in order to enhance catalytic performance in mesophilic host cells. Appl Environ Microbiol 2007, 73:6254-6261.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 6254-6261
    • Yoshida, S.1    Atomi, H.2    Imanaka, T.3
  • 35
    • 0038643328 scopus 로고    scopus 로고
    • Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in Archaea
    • Finn M.W., Tabita F.R. Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in Archaea. J Bacteriol 2003, 185:3049-3059.
    • (2003) J Bacteriol , vol.185 , pp. 3049-3059
    • Finn, M.W.1    Tabita, F.R.2
  • 36
    • 0035902973 scopus 로고    scopus 로고
    • Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
    • Dobbek H., Svetlitchnyi V., Gremer L., Huber R., Meyer O. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 2001, 293:1281-1285.
    • (2001) Science , vol.293 , pp. 1281-1285
    • Dobbek, H.1    Svetlitchnyi, V.2    Gremer, L.3    Huber, R.4    Meyer, O.5
  • 37
    • 20444377225 scopus 로고    scopus 로고
    • Energy generation from the CO oxidation-hydrogen production pathway in Rubrivivax gelatinosus
    • Maness P.C., Huang J., Smolinski S., Tek V., Vanzin G. Energy generation from the CO oxidation-hydrogen production pathway in Rubrivivax gelatinosus. Appl Environ Microbiol 2005, 71:2870-2874.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 2870-2874
    • Maness, P.C.1    Huang, J.2    Smolinski, S.3    Tek, V.4    Vanzin, G.5
  • 38
    • 0035667425 scopus 로고    scopus 로고
    • Evidence for three distinct hydrogenase activities in Rhodospirillum rubrum
    • Maness P.C., Weaver P.F. Evidence for three distinct hydrogenase activities in Rhodospirillum rubrum. Appl Microbiol Biotechnol 2001, 57:751-756.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 751-756
    • Maness, P.C.1    Weaver, P.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.