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Volumn 13, Issue 8, 2011, Pages 2232-2249

Chaperonins from an Antarctic archaeon are predominantly monomeric: Crystal structure of an open state monomer

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONIN; RECOMBINANT PROTEIN;

EID: 80051929084     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/j.1462-2920.2011.02477.x     Document Type: Article
Times cited : (7)

References (65)
  • 2
    • 70349456541 scopus 로고    scopus 로고
    • The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold-adaptation
    • Allen, M.A., Lauro, F.M., Williams, T.J., Burg, D.W., Siddiqui, K.S., De Franciscii, D., etal. (2009) The genome sequence of the psychrophilic archaeon, Methanococcoides burtonii: the role of genome evolution in cold-adaptation. ISME J 3: 1012-1035.
    • (2009) ISME J , vol.3 , pp. 1012-1035
    • Allen, M.A.1    Lauro, F.M.2    Williams, T.J.3    Burg, D.W.4    Siddiqui, K.S.5    De Franciscii, D.6
  • 4
    • 69849098012 scopus 로고    scopus 로고
    • A novel nucleoid-associated protein of Mycobacterium tuberculosis is a sequence homolog of GroEL
    • Basu, D., Khare, G., Singh, S., Tyagi, A., Khosla, S., and Mande, S.C. (2009) A novel nucleoid-associated protein of Mycobacterium tuberculosis is a sequence homolog of GroEL. Nucleic Acids Res 37: 4944-4954.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4944-4954
    • Basu, D.1    Khare, G.2    Singh, S.3    Tyagi, A.4    Khosla, S.5    Mande, S.C.6
  • 5
    • 0023922758 scopus 로고
    • Inorganic pyrophosphatase as a label in heterogeneous enzyme immunoassay
    • Baykov, A.A., Kasho, V.N., and Avaeva, S.M. (1988) Inorganic pyrophosphatase as a label in heterogeneous enzyme immunoassay. Anal Biochem 171: 271-276.
    • (1988) Anal Biochem , vol.171 , pp. 271-276
    • Baykov, A.A.1    Kasho, V.N.2    Avaeva, S.M.3
  • 6
    • 44549085390 scopus 로고    scopus 로고
    • Chaperonins: the hunt for the Group II mechanism
    • Bigotti, M.G., and Clarke, A.R. (2008) Chaperonins: the hunt for the Group II mechanism. Arch Biochem Biophys 474: 331-339.
    • (2008) Arch Biochem Biophys , vol.474 , pp. 331-339
    • Bigotti, M.G.1    Clarke, A.R.2
  • 8
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig, K., Adams, P.D., and Brunger, A.T. (1995) Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nat Struct Biol 2: 1083-1094.
    • (1995) Nat Struct Biol , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brunger, A.T.3
  • 9
    • 76149132993 scopus 로고    scopus 로고
    • Analyzing the hydrophobic proteome of the antarctic archaeon Methanococcoides burtonii using differential solubility fractionation
    • Burg, D.W., Lauro, F.M., Williams, T.J., Raftery, M.J., Guilhaus, M., and Cavicchioli, R. (2010) Analyzing the hydrophobic proteome of the antarctic archaeon Methanococcoides burtonii using differential solubility fractionation. J Proteome Res 9: 653-663.
    • (2010) J Proteome Res , vol.9 , pp. 653-663
    • Burg, D.W.1    Lauro, F.M.2    Williams, T.J.3    Raftery, M.J.4    Guilhaus, M.5    Cavicchioli, R.6
  • 10
    • 80051911251 scopus 로고    scopus 로고
    • Temperature-dependent global gene expression in the Antarctic archaeon, Methanococcoides burtonii
    • (in press): doi:10.1111/j.1462-2920.2010.02367.x.
    • Campanaro, S., Williams, T.J., De Francisci, D., Treu, L., Lauro, F.M., and Cavicchioli, R. (2011) Temperature-dependent global gene expression in the Antarctic archaeon, Methanococcoides burtonii. Environ Microbiol (in press): doi:10.1111/j.1462-2920.2010.02367.x.
    • (2011) Environ Microbiol
    • Campanaro, S.1    Williams, T.J.2    De Francisci, D.3    Treu, L.4    Lauro, F.M.5    Cavicchioli, R.6
  • 11
    • 33646839948 scopus 로고    scopus 로고
    • Cold-adapted archaea
    • Cavicchioli, R. (2006) Cold-adapted archaea. Nat Rev Microbiol 4: 331-343.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 331-343
    • Cavicchioli, R.1
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 - Collaborative Computational Project Number 4
    • CCP4 - Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 13
    • 0141754010 scopus 로고    scopus 로고
    • Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics
    • Chaudhry, C., Farr, G.W., Todd, M.J., Rye, H.S., Brunger, A.T., Adams, P.D., etal. (2003) Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. EMBO J 22: 4877-4887.
    • (2003) EMBO J , vol.22 , pp. 4877-4887
    • Chaudhry, C.1    Farr, G.W.2    Todd, M.J.3    Rye, H.S.4    Brunger, A.T.5    Adams, P.D.6
  • 14
    • 4143061452 scopus 로고    scopus 로고
    • Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states
    • Chaudhry, C., Horwich, A.L., Brunger, A.T., and Adams, P.D. (2004) Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states. J Mol Biol 342: 229-245.
    • (2004) J Mol Biol , vol.342 , pp. 229-245
    • Chaudhry, C.1    Horwich, A.L.2    Brunger, A.T.3    Adams, P.D.4
  • 16
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel, L., Lowe, J., Stock, D., Stetter, K.O., Huber, H., Huber, R., and Steinbacher, S. (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93: 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Stetter, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 17
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 18
    • 0038239271 scopus 로고    scopus 로고
    • Inactivation of the nod box distal half-site allowstetrameric NodD to activate nodA transcription in an inducer-independent manner
    • Feng, J., Li, Q., Hu, H.-L., Chen, X.-C., and Hong, G.-F. (2003) Inactivation of the nod box distal half-site allowstetrameric NodD to activate nodA transcription in an inducer-independent manner. Nucleic Acids Res 31: 3143-3156.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3143-3156
    • Feng, J.1    Li, Q.2    Hu, H.-L.3    Chen, X.-C.4    Hong, G.-F.5
  • 19
    • 0001522673 scopus 로고
    • Starch-gel electrophoresis-application to the classification of pituitary proteins and polypeptides
    • Ferguson, K.A. (1964) Starch-gel electrophoresis-application to the classification of pituitary proteins and polypeptides. Metabolism 13: 985-1002.
    • (1964) Metabolism , vol.13 , pp. 985-1002
    • Ferguson, K.A.1
  • 21
    • 0035929156 scopus 로고    scopus 로고
    • Crystal structure of chaperonin-60 from Paracoccus denitrificans
    • Fukami, T.A., Yohda, M., Taguchi, H., Yoshida, M., and Miki, K. (2001) Crystal structure of chaperonin-60 from Paracoccus denitrificans. J Mol Biol 312: 501-509.
    • (2001) J Mol Biol , vol.312 , pp. 501-509
    • Fukami, T.A.1    Yohda, M.2    Taguchi, H.3    Yoshida, M.4    Miki, K.5
  • 22
    • 0032561205 scopus 로고    scopus 로고
    • Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability
    • Furutani, M., Iida, T., Yoshida, T., and Maruyama, T. (1998) Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability. J Biol Chem 273: 28399-28407.
    • (1998) J Biol Chem , vol.273 , pp. 28399-28407
    • Furutani, M.1    Iida, T.2    Yoshida, T.3    Maruyama, T.4
  • 23
    • 43049164355 scopus 로고    scopus 로고
    • One dimensional electrophoresis using nondenaturing condtions
    • Gallagher, S.R. (2001) One dimensional electrophoresis using nondenaturing condtions. Curr Protocols Protein Sci: 10.3.1-10.3.11.
    • (2001) Curr Protocols Protein Sci , pp. 1031-10311
    • Gallagher, S.R.1
  • 24
    • 0026518296 scopus 로고
    • A modified colorimetric method for the determination of orthophosphate in the presence of high ATP concentrations
    • Gonzalez-Romo, P., Sanchez-Nieto, S., and Gavilanes-Ruiz, M. (1992) A modified colorimetric method for the determination of orthophosphate in the presence of high ATP concentrations. Anal Biochem 200: 235-238.
    • (1992) Anal Biochem , vol.200 , pp. 235-238
    • Gonzalez-Romo, P.1    Sanchez-Nieto, S.2    Gavilanes-Ruiz, M.3
  • 25
    • 10044245551 scopus 로고    scopus 로고
    • Biology of the cold adapted archaeon, Methanococcoides burtonii determined by proteomics using liquid chromatography-tandem mass spectrometry
    • Goodchild, A., Raftery, M., Saunders, N.F.W., Guilhaus, M., and Cavicchioli, R. (2004a) Biology of the cold adapted archaeon, Methanococcoides burtonii determined by proteomics using liquid chromatography-tandem mass spectrometry. J Proteome Res 3: 1164-1176.
    • (2004) J Proteome Res , vol.3 , pp. 1164-1176
    • Goodchild, A.1    Raftery, M.2    Saunders, N.F.W.3    Guilhaus, M.4    Cavicchioli, R.5
  • 27
    • 17444384908 scopus 로고    scopus 로고
    • Cold adaptation of the Antarctic archaeon, Methanococcoides burtonii assessed by proteomics using ICAT
    • Goodchild, A., Raftery, M., Saunders, N.F., Guilhaus, M., and Cavicchioli, R. (2005) Cold adaptation of the Antarctic archaeon, Methanococcoides burtonii assessed by proteomics using ICAT. J Proteome Res 4: 473-480.
    • (2005) J Proteome Res , vol.4 , pp. 473-480
    • Goodchild, A.1    Raftery, M.2    Saunders, N.F.3    Guilhaus, M.4    Cavicchioli, R.5
  • 28
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl, F.U., and Hayer-Hartl, M. (2009) Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16: 574-581.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 29
    • 77957786479 scopus 로고    scopus 로고
    • Crystal structure of group II chaperonin in the open state
    • Huo, Y., Hu, Z., Zhang, K., Wang, L., Zhai, Y., Zhou, Q., etal. (2010) Crystal structure of group II chaperonin in the open state. Structure 18: 1270-1279.
    • (2010) Structure , vol.18 , pp. 1270-1279
    • Huo, Y.1    Hu, Z.2    Zhang, K.3    Wang, L.4    Zhai, Y.5    Zhou, Q.6
  • 30
    • 34249939993 scopus 로고    scopus 로고
    • Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions
    • Kiser, P.D., Lodowski, D.T., and Palczewski, K. (2007) Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions. Acta Crystallograph Sect F Struct Biol Cryst Commun 63: 457-461.
    • (2007) Acta Crystallograph Sect F Struct Biol Cryst Commun , vol.63 , pp. 457-461
    • Kiser, P.D.1    Lodowski, D.T.2    Palczewski, K.3
  • 31
    • 0042357157 scopus 로고    scopus 로고
    • Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei
    • Klunker, D., Haas, B., Hirtreiter, A., Figueiredo, L., Naylor, D.J., Pfeifer, G., etal. (2003) Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei. J Biol Chem 278: 33256-33267.
    • (2003) J Biol Chem , vol.278 , pp. 33256-33267
    • Klunker, D.1    Haas, B.2    Hirtreiter, A.3    Figueiredo, L.4    Naylor, D.J.5    Pfeifer, G.6
  • 32
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S., and Wilson, K.S. (1993) Automated refinement of protein models. Acta Crystallogr D 49: 129-149.
    • (1993) Acta Crystallogr D , vol.49 , pp. 129-149
    • Lamzin, V.S.1    Wilson, K.S.2
  • 33
    • 63849276112 scopus 로고    scopus 로고
    • Archaeal chaperonins
    • Large, A.T., and Lund, P.A. (2009) Archaeal chaperonins. Front Biosci 14: 1304-1324.
    • (2009) Front Biosci , vol.14 , pp. 1304-1324
    • Large, A.T.1    Lund, P.A.2
  • 34
    • 0037132503 scopus 로고    scopus 로고
    • Properties of the chaperonin complex from the halophilic archaeon Haloferax volcanii
    • Large, A.T., Kovacs, E., and Lund, P.A. (2002) Properties of the chaperonin complex from the halophilic archaeon Haloferax volcanii. FEBS Lett 532: 309-312.
    • (2002) FEBS Lett , vol.532 , pp. 309-312
    • Large, A.T.1    Kovacs, E.2    Lund, P.A.3
  • 35
    • 59749085330 scopus 로고    scopus 로고
    • Chaperones and protein folding in the archaea
    • Large, A.T., Goldberg, M.D., and Lund, P.A. (2009) Chaperones and protein folding in the archaea. Biochem Soc Trans 37: 46-51.
    • (2009) Biochem Soc Trans , vol.37 , pp. 46-51
    • Large, A.T.1    Goldberg, M.D.2    Lund, P.A.3
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: a program to check stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1994) PROCHECK: a program to check stereochemical quality of protein structures. J Appl Crystsallogr 26: 283-291.
    • (1994) J Appl Crystsallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 39
    • 39149087390 scopus 로고    scopus 로고
    • Diversity and genomics of Antarctic marine micro-organisms
    • Murray, A.E., and Grzymski, J.J. (2007) Diversity and genomics of Antarctic marine micro-organisms. Philos Trans R Soc Lond B Biol Sci 362: 2259-2271.
    • (2007) Philos Trans R Soc Lond B Biol Sci , vol.362 , pp. 2259-2271
    • Murray, A.E.1    Grzymski, J.J.2
  • 40
    • 18644378418 scopus 로고    scopus 로고
    • Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3
    • Okochi, M., Matsuzaki, H., Nomura, T., Ishii, N., and Yohda, M. (2005) Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3. Extremophiles 9: 127-134.
    • (2005) Extremophiles , vol.9 , pp. 127-134
    • Okochi, M.1    Matsuzaki, H.2    Nomura, T.3    Ishii, N.4    Yohda, M.5
  • 41
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: an application to display phylogenetic trees on personal computers
    • Page, R.D. (1996) TreeView: an application to display phylogenetic trees on personal computers. Comput Appl Biosci 12: 357-358.
    • (1996) Comput Appl Biosci , vol.12 , pp. 357-358
    • Page, R.D.1
  • 42
    • 77956256437 scopus 로고    scopus 로고
    • Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle
    • Pereira, J.H., Ralston, C.Y., Douglas, N., Meyer, D., Knee, K.M., Goulet, D.R., etal. (2010) Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle. J Biol Chem 285: 27958-27966.
    • (2010) J Biol Chem , vol.285 , pp. 27958-27966
    • Pereira, J.H.1    Ralston, C.Y.2    Douglas, N.3    Meyer, D.4    Knee, K.M.5    Goulet, D.R.6
  • 43
    • 63649139204 scopus 로고    scopus 로고
    • Peptide quantification using 8-plex isobaric tags and electron transfer dissociation tandem mass spectrometry
    • Phanstiel, D., Unwin, R., McAlister, G.C., and Coon, J.J. (2009) Peptide quantification using 8-plex isobaric tags and electron transfer dissociation tandem mass spectrometry. Anal Chem 81: 1693-1698.
    • (2009) Anal Chem , vol.81 , pp. 1693-1698
    • Phanstiel, D.1    Unwin, R.2    McAlister, G.C.3    Coon, J.J.4
  • 44
    • 9244227956 scopus 로고    scopus 로고
    • Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis
    • Qamra, R., and Mande, S.C. (2004) Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis. J Bacteriol 186: 8105-8113.
    • (2004) J Bacteriol , vol.186 , pp. 8105-8113
    • Qamra, R.1    Mande, S.C.2
  • 45
    • 4344587654 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins
    • Qamra, R., Srinivas, V., and Mande, S.C. (2004) Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins. J Mol Biol 342: 605-617.
    • (2004) J Mol Biol , vol.342 , pp. 605-617
    • Qamra, R.1    Srinivas, V.2    Mande, S.C.3
  • 47
    • 33750338843 scopus 로고    scopus 로고
    • Terrestrial models for extraterrestrial life: methanogens and halophiles at Martian temperatures
    • Reid, I.N., Sparks, W.B., Lubnow, S., McGrath, M., Livio, M., Valenti, J., etal. (2006) Terrestrial models for extraterrestrial life: methanogens and halophiles at Martian temperatures. Int J Astrobiol 5: 89-97.
    • (2006) Int J Astrobiol , vol.5 , pp. 89-97
    • Reid, I.N.1    Sparks, W.B.2    Lubnow, S.3    McGrath, M.4    Livio, M.5    Valenti, J.6
  • 48
    • 0032526978 scopus 로고    scopus 로고
    • The chaperonin of the archaeon Sulfolobus solfataricus is an RNA-binding protein that participates in ribosomal RNA processing
    • Ruggero, D., Ciammaruconi, A., and Londei, P. (1998) The chaperonin of the archaeon Sulfolobus solfataricus is an RNA-binding protein that participates in ribosomal RNA processing. EMBO J 17: 3471-3477.
    • (1998) EMBO J , vol.17 , pp. 3471-3477
    • Ruggero, D.1    Ciammaruconi, A.2    Londei, P.3
  • 49
    • 0036899202 scopus 로고    scopus 로고
    • The chaperonin folding machine
    • Saibil, H.R., and Ranson, N.A. (2002) The chaperonin folding machine. Trends Biochem Sci 27: 627-632.
    • (2002) Trends Biochem Sci , vol.27 , pp. 627-632
    • Saibil, H.R.1    Ranson, N.A.2
  • 50
    • 17444376059 scopus 로고    scopus 로고
    • Predicted roles for hypothetical proteins in the low-temperature expressed proteome of the Antarctic archaeon Methanococcoides burtonii
    • Saunders, N.F.W., Goodchild, A., Raftery, M., Guilhaus, M., Curmi, P.M.G., and Cavicchioli, R. (2005) Predicted roles for hypothetical proteins in the low-temperature expressed proteome of the Antarctic archaeon Methanococcoides burtonii. J Proteome Res 4: 464-472.
    • (2005) J Proteome Res , vol.4 , pp. 464-472
    • Saunders, N.F.W.1    Goodchild, A.2    Raftery, M.3    Guilhaus, M.4    Curmi, P.M.G.5    Cavicchioli, R.6
  • 51
    • 33748333118 scopus 로고    scopus 로고
    • Proteomic and computational analysis of secreted proteins with type I signal peptides from the Antarctic archaeon Methanococcoides burtonii
    • Saunders, N.F.W., Ng, C., Raftery, M., Guilhaus, M., Goodchild, A., and Cavicchioli, R. (2006) Proteomic and computational analysis of secreted proteins with type I signal peptides from the Antarctic archaeon Methanococcoides burtonii. J Proteome Res 5: 2457-2464.
    • (2006) J Proteome Res , vol.5 , pp. 2457-2464
    • Saunders, N.F.W.1    Ng, C.2    Raftery, M.3    Guilhaus, M.4    Goodchild, A.5    Cavicchioli, R.6
  • 52
    • 0034636980 scopus 로고    scopus 로고
    • Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin
    • Schoehn, G., Hayes, M., Cliff, M., Clarke, A.R., and Saibil, H.R. (2000a) Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin. J Mol Biol 301: 323-332.
    • (2000) J Mol Biol , vol.301 , pp. 323-332
    • Schoehn, G.1    Hayes, M.2    Cliff, M.3    Clarke, A.R.4    Saibil, H.R.5
  • 53
    • 0034711948 scopus 로고    scopus 로고
    • Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae
    • Schoehn, G., Quaite-Randall, E., Jimenez, J.L., Joachimiak, A., and Saibil, H.R. (2000b) Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae. J Mol Biol 296: 813-819.
    • (2000) J Mol Biol , vol.296 , pp. 813-819
    • Schoehn, G.1    Quaite-Randall, E.2    Jimenez, J.L.3    Joachimiak, A.4    Saibil, H.R.5
  • 54
    • 4143134164 scopus 로고    scopus 로고
    • Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
    • Shimamura, T., Koike-Takeshita, A., Yokoyama, K., Masui, R., Murai, N., Yoshida, M., etal. (2004) Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure 12: 1471-1480.
    • (2004) Structure , vol.12 , pp. 1471-1480
    • Shimamura, T.1    Koike-Takeshita, A.2    Yokoyama, K.3    Masui, R.4    Murai, N.5    Yoshida, M.6
  • 55
    • 0347757092 scopus 로고    scopus 로고
    • Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms
    • Shomura, Y., Yoshida, T., Iizuka, R., Maruyama, T., Yohda, M., and Miki, K. (2004) Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms. J Mol Biol 335: 1265-1278.
    • (2004) J Mol Biol , vol.335 , pp. 1265-1278
    • Shomura, Y.1    Yoshida, T.2    Iizuka, R.3    Maruyama, T.4    Yohda, M.5    Miki, K.6
  • 56
    • 68149149564 scopus 로고    scopus 로고
    • UROX 2.0: an interactive tool for fitting atomic models into electron-microscopy reconstructions
    • Siebert, X., and Navaza, J. (2009) UROX 2.0: an interactive tool for fitting atomic models into electron-microscopy reconstructions. Acta Crystallogr D Biol Crystallogr 65: 651-658.
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , pp. 651-658
    • Siebert, X.1    Navaza, J.2
  • 58
    • 0037418665 scopus 로고    scopus 로고
    • Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0Å resolution
    • Wang, J., and Boisvert, D.C. (2003) Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0Å resolution. J Mol Biol 327: 843-855.
    • (2003) J Mol Biol , vol.327 , pp. 843-855
    • Wang, J.1    Boisvert, D.C.2
  • 59
    • 0242493845 scopus 로고    scopus 로고
    • Domain motions in GroEL upon binding of an oligopeptide
    • Wang, J., and Chen, L. (2003) Domain motions in GroEL upon binding of an oligopeptide. J Mol Biol 334: 489-499.
    • (2003) J Mol Biol , vol.334 , pp. 489-499
    • Wang, J.1    Chen, L.2
  • 60
    • 76149124222 scopus 로고    scopus 로고
    • Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii Part I: the effect of growth temperature
    • Williams, T.J., Burg, D.W., Raftery, M.J., Poljak, A., Guilhaus, M., Pilak, O., and Cavicchioli, R. (2010a) Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii Part I: the effect of growth temperature. J Proteome Res 9: 640-652.
    • (2010) J Proteome Res , vol.9 , pp. 640-652
    • Williams, T.J.1    Burg, D.W.2    Raftery, M.J.3    Poljak, A.4    Guilhaus, M.5    Pilak, O.6    Cavicchioli, R.7
  • 61
    • 76149128021 scopus 로고    scopus 로고
    • Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii Part II: the effect of different methylated growth substrates
    • Williams, T.J., Burg, D.W., Ertan, H., Raftery, M.J., Poljak, A., Guilhaus, M., and Cavicchioli, R. (2010b) Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii Part II: the effect of different methylated growth substrates. J Proteome Res 9: 653-663.
    • (2010) J Proteome Res , vol.9 , pp. 653-663
    • Williams, T.J.1    Burg, D.W.2    Ertan, H.3    Raftery, M.J.4    Poljak, A.5    Guilhaus, M.6    Cavicchioli, R.7
  • 62
    • 80051944885 scopus 로고    scopus 로고
    • Defining the response of a microorganism to growth semperature that spans its full growth temperature range (-2°C to 28°C) using multiplex quantitative proteomics
    • (in press): doi:10.1111/j.1462-2920.2011.02467.x.
    • Williams, T.J., Lauro, F.M., Ertan, H., Burg, D., Poljak, A., Raftery, M.J., and Cavicchioli, R. (2011) Defining the response of a microorganism to growth semperature that spans its full growth temperature range (-2°C to 28°C) using multiplex quantitative proteomics. Environ Microbiol (in press): doi:10.1111/j.1462-2920.2011.02467.x.
    • (2011) Environ Microbiol
    • Williams, T.J.1    Lauro, F.M.2    Ertan, H.3    Burg, D.4    Poljak, A.5    Raftery, M.J.6    Cavicchioli, R.7
  • 63
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES- (ADP)7 chaperonin complex
    • Xu, Z., Horwich, A.L., and Sigler, P.B. (1997) The crystal structure of the asymmetric GroEL-GroES- (ADP)7 chaperonin complex. Nature 388: 741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 64
    • 0036093758 scopus 로고    scopus 로고
    • Two kinds of archaeal group II chaperonin subunits with different thermostability in Thermococcus strain KS-1
    • Yoshida, T., Ideno, A., Suzuki, R., Yohda, M., and Maruyama, T. (2002) Two kinds of archaeal group II chaperonin subunits with different thermostability in Thermococcus strain KS-1. Mol Microbiol 44: 761-769.
    • (2002) Mol Microbiol , vol.44 , pp. 761-769
    • Yoshida, T.1    Ideno, A.2    Suzuki, R.3    Yohda, M.4    Maruyama, T.5


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