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Volumn 151, Issue 4, 2012, Pages 383-390

Varied effects of Pyrococcus furiosus prefoldin and P. furiosus chaperonin on the refolding reactions of substrate proteins

Author keywords

chaperonin; citrate synthase; prefoldin; protein folding; Pyrococcus furiosus

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CHAPERONIN; CITRATE SYNTHASE; ENHANCED GREEN FLUORESCENT PROTEIN; PYROCOCCUS FURIOSUS PREFOLDIN; UNCLASSIFIED DRUG;

EID: 84859308984     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr141     Document Type: Article
Times cited : (4)

References (38)
  • 1
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis, J. (1987) Proteins as molecular chaperones. Nature 328, 378-379
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature 381, 571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 3
    • 33749538453 scopus 로고    scopus 로고
    • Convergent evolution of clamp-like binding sites in diverse chaperones
    • DOI 10.1038/nsmb1153, PII NSMB1153
    • Stirling, P.C., Bakhoum, S.F., Feigl, A.B., and Leroux, M.R. (2006) Convergent evolution of clamp-like binding sites in diverse chaperones. Nat. Struct. Mol. Biol 13, 865-870 (Pubitemid 44527367)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.10 , pp. 865-870
    • Stirling, P.C.1    Bakhoum, S.F.2    Feigl, A.B.3    Leroux, M.R.4
  • 4
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • Hartl, F.U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858 (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 6
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • DOI 10.1016/j.tcb.2004.09.015, PII S0962892404002661
    • Spiess, C., Meyer, A.S., Reissmann, S., and Frydman, J. (2004) Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol 14, 598-604 (Pubitemid 39440608)
    • (2004) Trends in Cell Biology , vol.14 , Issue.11 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 7
    • 68649123756 scopus 로고    scopus 로고
    • The GroEL/GroES cis cavity as a passive anti-aggregation device
    • Horwich, A.L., Apetri, A.C., and Fenton, W.A. (2009) The GroEL/GroES cis cavity as a passive anti-aggregation device. FEBS Lett. 583, 2654-2662
    • (2009) FEBS Lett. , vol.583 , pp. 2654-2662
    • Horwich, A.L.1    Apetri, A.C.2    Fenton, W.A.3
  • 8
    • 0035929150 scopus 로고    scopus 로고
    • Chaperonins - Keeping a lid on folding proteins
    • DOI 10.1016/S0014-5793(01)02838-1, PII S0014579301028381
    • Kusmierczyk, A.R. and Martin, J. (2001) Chaperonins - keeping a lid on folding proteins. FEBS Lett. 505, 343-347 (Pubitemid 32905474)
    • (2001) FEBS Letters , vol.505 , Issue.3 , pp. 343-347
    • Kusmierczyk, A.R.1    Martin, J.2
  • 9
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • DOI 10.1093/emboj/18.1.75
    • Siegers, K., Waldmann, T., Leroux, M.R., Grein, K., Shevchenko, A., Schiebel, E., and Hartl, F.U. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18, 75-84 (Pubitemid 29005025)
    • (1999) EMBO Journal , vol.18 , Issue.1 , pp. 75-84
    • Siegers, K.1    Waldmann, T.2    Leroux, M.R.3    Grein, K.4    Shevchenko, A.5    Schiebel, E.6    Hartl, F.U.7
  • 10
    • 0032577573 scopus 로고    scopus 로고
    • Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
    • DOI 10.1016/S0092-8674(00)81446-4
    • Vainberg, I.E., Lewis, S.A., Rommelaere, H., Ampe, C., Vandekerckhove, J., Klein, H.L., and Cowan, N.J. (1998) Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93, 863-873 (Pubitemid 28257591)
    • (1998) Cell , vol.93 , Issue.5 , pp. 863-873
    • Vainberg, I.E.1    Lewis, S.A.2    Rommelaere, H.3    Ampe, C.4    Vandekerckhove, J.5    Klein, H.L.6    Cowan, N.J.7
  • 11
    • 0345518025 scopus 로고    scopus 로고
    • Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
    • DOI 10.1083/jcb.145.2.265
    • Hansen, W.J., Cowan, N.J., and Welch, W.J. (1999) Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J Cell Biol 145, 265-277 (Pubitemid 29198300)
    • (1999) Journal of Cell Biology , vol.145 , Issue.2 , pp. 265-277
    • Hansen, W.J.1    Cowan, N.J.2    Welch, W.J.3
  • 13
    • 50049129343 scopus 로고    scopus 로고
    • Expression profiles and physiological roles of two types of prefoldins from the hyperthermophilic archaeon Thermococcus kodakaraensis
    • Danno, A., Fukuda, W., Yoshida, M., Aki, R., Tanaka, T., Kanai, T., Imanaka, T., and Fujiwara, S. (2008) Expression profiles and physiological roles of two types of prefoldins from the hyperthermophilic archaeon Thermococcus kodakaraensis. J Mol Biol 382, 298-311
    • (2008) J Mol Biol , vol.382 , pp. 298-311
    • Danno, A.1    Fukuda, W.2    Yoshida, M.3    Aki, R.4    Tanaka, T.5    Kanai, T.6    Imanaka, T.7    Fujiwara, S.8
  • 14
    • 40649126526 scopus 로고    scopus 로고
    • Functional characterization of recombinant prefoldin complexes from a hyperthermophilic archaeon, Thermococcus sp. strain KS-1
    • Iizuka, R., Sugano, Y., Ide, N., Ohtaki, A., Yoshida, T., Fujiwara, S., Imanaka, T., and Yohda, M. (2008) Functional characterization of recombinant prefoldin complexes from a hyperthermophilic archaeon, Thermococcus sp. strain KS-1. J Mol Biol 377, 972-983
    • (2008) J Mol Biol , vol.377 , pp. 972-983
    • Iizuka, R.1    Sugano, Y.2    Ide, N.3    Ohtaki, A.4    Yoshida, T.5    Fujiwara, S.6    Imanaka, T.7    Yohda, M.8
  • 15
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional alpha- and gamma-tubulin
    • DOI 10.1093/emboj/17.4.952
    • Geissler, S., Siegers, K., and Schiebel, E. (1998) A novel protein complex promoting formation of functional alpha- and gamma-tubulin. EMBO J. 17, 952-966 (Pubitemid 28077650)
    • (1998) EMBO Journal , vol.17 , Issue.4 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 17
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert, R., Leroux, M.R., Scheufler, C., Hartl, F.U., and Moarefi, I. (2000) Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621-632
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 18
    • 0032956536 scopus 로고    scopus 로고
    • Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferred from this protein
    • Gribaldo, S., Lumia, V., Creti, R., de Macario, E.C., Sanangelantoni, A., and Cammarano, P. (1999) Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferred from this protein. J. Bacteriol. 181, 434-443 (Pubitemid 29045133)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 434-443
    • Gribaldo, S.1    Lumia, V.2    Creti, R.3    Conway, D.M.E.4    Sanangelantoni, A.5    Cammarano, P.6
  • 19
    • 0344500848 scopus 로고    scopus 로고
    • The archaeal molecular chaperone machine: Peculiarities and paradoxes
    • Macario, A.J. and de Macario, E.C. (1999) The archaeal molecular chaperone machine: peculiarities and paradoxes. Genetics 152, 1277-1283 (Pubitemid 29370311)
    • (1999) Genetics , vol.152 , Issue.4 , pp. 1277-1283
    • Macario, A.J.L.1    Conway, D.M.E.2
  • 20
    • 2142806742 scopus 로고    scopus 로고
    • Minimal protein-folding systems in hyperthermophilic archaea
    • DOI 10.1038/nrmicro866
    • Laksanalamai, P., Whitehead, T.A., and Robb, F.T. (2004) Minimal protein-folding systems in hyperthermophilic archaea. Nat. Rev. Microbiol. 2, 315-324 (Pubitemid 39490101)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.4 , pp. 315-324
    • Laksanalamai, P.1    Whitehead, T.A.2    Robb, F.T.3
  • 24
    • 29344467429 scopus 로고    scopus 로고
    • A novel ATP/ADP hydrolysis activity of hyperthermostable group II chaperonin in the presence of cobalt or manganese ion
    • DOI 10.1016/j.febslet.2005.11.043, PII S0014579305014122
    • Hongo, K., Hirai, H., Uemura, C., Ono, S., Tsunemi, J., Higurashi, T., Mizobata, T., and Kawata, Y. (2006) A novel ATP/ADP hydrolysis activity of hyperthermostable group II chaperonin in the presence of cobalt or manganese ion. FEBS Lett. 580, 34-40 (Pubitemid 43005308)
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 34-40
    • Hongo, K.1    Hirai, H.2    Uemura, C.3    Ono, S.4    Tsunemi, J.5    Higurashi, T.6    Mizobata, T.7    Kawata, Y.8
  • 25
    • 0344604534 scopus 로고    scopus 로고
    • Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences
    • Maeder, D.L., Weiss, R.B., Dunn, D.M., Cherry, J.L., Gonzalez, J.M., DiRuggiero, J., and Robb, F.T. (1999) Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences. Genetics 152, 1299-1305
    • (1999) Genetics , vol.152 , pp. 1299-1305
    • Maeder, D.L.1    Weiss, R.B.2    Dunn, D.M.3    Cherry, J.L.4    Gonzalez, J.M.5    DiRuggiero, J.6    Robb, F.T.7
  • 26
    • 0029116222 scopus 로고
    • Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus
    • Muir, J.M., Russell, R.J., Hough, D.W., and Danson, M.J. (1995) Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus. Protein Eng. 8, 583-592
    • (1995) Protein Eng. , vol.8 , pp. 583-592
    • Muir, J.M.1    Russell, R.J.2    Hough, D.W.3    Danson, M.J.4
  • 27
    • 1942469376 scopus 로고    scopus 로고
    • Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain: Relationships between movements in the apical domain and the quaternary structure of GroEL
    • DOI 10.1074/jbc.M311806200
    • Taniguchi, M., Yoshimi, T., Hongo, K., Mizobata, T., and Kawata, Y. (2004) Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain: relationships between movements in the apical domain and the quaternary structure of GroEL. J. Biol. Chem. 279, 16368-16376 (Pubitemid 38509333)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16368-16376
    • Taniguchi, M.1    Yoshimi, T.2    Hongo, K.3    Mizobata, T.4    Kawata, Y.5
  • 28
    • 41349108000 scopus 로고    scopus 로고
    • Functional characterization of the recombinant group II chaperonin alpha from Thermoplasma acidophilum
    • DOI 10.1093/jb/mvm241
    • Hirai, H., Noi, K., Hongo, K., Mizobata, T., and Kawata, Y. (2008) Functional characterization of the recombinant group II chaperonin alpha from Thermoplasma acidophilum. J. Biochem. 143, 505-515 (Pubitemid 351451764)
    • (2008) Journal of Biochemistry , vol.143 , Issue.4 , pp. 505-515
    • Hirai, H.1    Noi, K.2    Hongo, K.3    Mizobata, T.4    Kawata, Y.5
  • 29
    • 0001647511 scopus 로고
    • The citrate condensing enzyme of pigeon breast muscle and moth flight muscle
    • Srere, P.A., Brazil, H., and Gonen, L. (1963) The citrate condensing enzyme of pigeon breast muscle and moth flight muscle. Acta Chem. Scand. 17, S129-S134
    • (1963) Acta Chem. Scand. , vol.17
    • Srere, P.A.1    Brazil, H.2    Gonen, L.3
  • 30
    • 70350270024 scopus 로고    scopus 로고
    • Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus
    • Chen, H.Y., Tan, X.L., Lu, J., Zhang, C.X., Zhang, Y., and Yang, S.L. (2009) Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus. Biotechnol. Lett. 31, 1753-1758
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1753-1758
    • Chen, H.Y.1    Tan, X.L.2    Lu, J.3    Zhang, C.X.4    Zhang, Y.5    Yang, S.L.6
  • 31
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • DOI 10.1016/0003-2697(79)90115-5
    • Lanzetta, P.A., Alvarez, L.J., Reinach, P.S., and Candia, O.A. (1979) An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100, 95-97 (Pubitemid 10157636)
    • (1979) Analytical Biochemistry , vol.100 , Issue.1 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 32
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., Whitehorn, E.A., Tate, E., and Stemmer, W.P. (1996) Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14, 315-319
    • (1996) Nat. Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 33
    • 0032788447 scopus 로고    scopus 로고
    • Circularly permuted variants of the green fluorescent protein
    • DOI 10.1016/S0014-5793(99)01044-3, PII S0014579399010443
    • Topell, S., Hennecke, J., and Glockshuber, R. (1999) Circularly permuted variants of the green fluorescent protein. FEBS Lett. 457, 283-289 (Pubitemid 29401943)
    • (1999) FEBS Letters , vol.457 , Issue.2 , pp. 283-289
    • Topell, S.1    Hennecke, J.2    Glockshuber, R.3
  • 34
    • 0027308741 scopus 로고
    • Eukaryotic homologues of Escherichia coli dnaJ: A diverse protein family that functions with HSP70 stress proteins
    • Caplan, A.J., Cyr, D.M., and Douglas, M.G. (1993) Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins. Mol Biol Cell 4, 555-563 (Pubitemid 23183603)
    • (1993) Molecular Biology of the Cell , vol.4 , Issue.6 , pp. 555-563
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 35
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta-actin folding
    • Gao, Y., Thomas, J.O., Chow, R.L., Lee, G.H., and Cowan, N.J. (1992) A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 69, 1043-1050
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 36
    • 34250177622 scopus 로고    scopus 로고
    • Expression and characterization of the chaperonin molecular machine from the hyperthermophilic archaeon Pyrococcus furiosus
    • DOI 10.1002/jobm.200610215
    • Chen, H.Y., Chu, Z.M., Ma, Y.H., Zhang, Y., and Yang, S.L. (2007) Expression and characterization of the chaperonin molecular machine from the hyperthermophilic archaeon Pyrococcus furiosus. J. Basic Microbiol. 47, 132-137 (Pubitemid 46953812)
    • (2007) Journal of Basic Microbiology , vol.47 , Issue.2 , pp. 132-137
    • Chen, H.-Y.1    Chu, Z.-M.2    Ma, Y.-H.3    Zhang, Y.4    Yang, S.-L.5
  • 37
    • 67349208011 scopus 로고    scopus 로고
    • An exceptionally stable Group II chaperonin from the hyperthermophile Pyrococcus furiosus
    • Luo, H., Laksanalamai, P., and Robb, F.T. (2009) An exceptionally stable Group II chaperonin from the hyperthermophile Pyrococcus furiosus. Arch. Biochem. Biophys. 486, 12-18
    • (2009) Arch. Biochem. Biophys. , vol.486 , pp. 12-18
    • Luo, H.1    Laksanalamai, P.2    Robb, F.T.3
  • 38
    • 18644378418 scopus 로고    scopus 로고
    • Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3
    • DOI 10.1007/s00792-004-0427-y
    • 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 (Pubitemid 40660352)
    • (2005) Extremophiles , vol.9 , Issue.2 , pp. 127-134
    • Okochi, M.1    Matsuzaki, H.2    Nomura, T.3    Ishii, N.4    Yohda, M.5


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