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Volumn 377, Issue 3, 2008, Pages 972-983

Functional Characterization of Recombinant Prefoldin Complexes from a Hyperthermophilic Archaeon, Thermococcus sp. Strain KS-1

Author keywords

archaea; chaperone; group II chaperonin; prefoldin; Thermococcus

Indexed keywords

CHAPERONIN; PREFOLDIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 40649126526     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.070     Document Type: Article
Times cited : (22)

References (37)
  • 1
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional alpha- and gamma-tubulin
    • S. Geissler K. Siegers E. Schiebel A novel protein complex promoting formation of functional alpha- and gamma-tubulin EMBO J. 17 1998 952 966
    • (1998) EMBO J. , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 3
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins
    • R. Siegert M.R. Leroux C. Scheufler F.U. Hartl I. Moarefi Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins Cell 103 2000 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
  • 4
    • 0345201713 scopus 로고    scopus 로고
    • MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin
    • M.R. Leroux M. Fandrich D. Klunker K. Siegers A.N. Lupas J.R. Brown MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin EMBO J. 18 1999 6730 6743
    • (1999) EMBO J. , vol.18 , pp. 6730-6743
    • Leroux, M.R.1    Fandrich, M.2    Klunker, D.3    Siegers, K.4    Lupas, A.N.5    Brown, J.R.6
  • 5
    • 0037011162 scopus 로고    scopus 로고
    • Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT
    • J. Martin-Benito J. Boskovic P. Gomez-Puertas J.L. Carrascosa C.T. Simons S.A. Lewis Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT EMBO J. 21 2002 6377 6386
    • (2002) EMBO J. , vol.21 , pp. 6377-6386
    • Martin-Benito, J.1    Boskovic, J.2    Gomez-Puertas, P.3    Carrascosa, J.L.4    Simons, C.T.5    Lewis, S.A.6
  • 6
    • 33846238951 scopus 로고    scopus 로고
    • Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart
    • J. Martin-Benito J. Gomez-Reino P.C. Stirling V.F. Lundin P. Gomez-Puertas J. Boskovic Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart Structure 15 2007 101 110
    • (2007) Structure , vol.15 , pp. 101-110
    • Martin-Benito, J.1    Gomez-Reino, J.2    Stirling, P.C.3    Lundin, V.F.4    Gomez-Puertas, P.5    Boskovic, J.6
  • 7
    • 3843093899 scopus 로고    scopus 로고
    • Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin
    • M. Okochi T. Nomura T. Zako T. Arakawa R. Iizuka H. Ueda Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin J. Biol. Chem. 279 2004 31788 31795
    • (2004) J. Biol. Chem. , vol.279 , pp. 31788-31795
    • Okochi, M.1    Nomura, T.2    Zako, T.3    Arakawa, T.4    Iizuka, R.5    Ueda, H.6
  • 8
    • 1042278172 scopus 로고    scopus 로고
    • Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding
    • C.T. Simons A. Staes H. Rommelaere C. Ampe S.A. Lewis N.J. Cowan Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding J. Biol. Chem. 279 2004 4196 4203
    • (2004) J. Biol. Chem. , vol.279 , pp. 4196-4203
    • Simons, C.T.1    Staes, A.2    Rommelaere, H.3    Ampe, C.4    Lewis, S.A.5    Cowan, N.J.6
  • 9
    • 0345518025 scopus 로고    scopus 로고
    • Prefoldin–nascent chain complexes in the folding of cytoskeletal proteins
    • W.J. Hansen N.J. Cowan W.J. Welch Prefoldin–nascent chain complexes in the folding of cytoskeletal proteins J. Cell Biol. 145 1999 265 277
    • (1999) J. Cell Biol. , vol.145 , pp. 265-277
    • Hansen, W.J.1    Cowan, N.J.2    Welch, W.J.3
  • 10
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin–GimC system
    • K. Siegers T. Waldmann M.R. Leroux K. Grein A. Shevchenko E. Schiebel F.U. Hartl Compartmentation of protein folding in vivo : sequestration of non-native polypeptide by the chaperonin–GimC system EMBO J. 18 1999 75 84
    • (1999) EMBO J. , vol.18 , 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
  • 11
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • V. Albanese A.Y. Yam J. Baughman C. Parnot J. Frydman Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells Cell 124 2006 75 88
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanese, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 12
    • 0036299118 scopus 로고    scopus 로고
    • Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding
    • M. Okochi T. Yoshida T. Maruyama Y. Kawarabayasi H. Kikuchi M. Yohda Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding Biochem. Biophys. Res. Commun. 291 2002 769 774
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 769-774
    • Okochi, M.1    Yoshida, T.2    Maruyama, T.3    Kawarabayasi, Y.4    Kikuchi, H.5    Yohda, M.6
  • 15
    • 2442704477 scopus 로고    scopus 로고
    • Archaeal peptidyl prolyl cis–trans isomerases (PPIases) update 2004
    • T. Maruyama R. Suzuki M. Furutani Archaeal peptidyl prolyl cis – trans isomerases (PPIases) update 2004 Front. Biosci. 9 2004 1680 1720
    • (2004) Front. Biosci. , vol.9 , pp. 1680-1720
    • Maruyama, T.1    Suzuki, R.2    Furutani, M.3
  • 16
    • 0031592944 scopus 로고    scopus 로고
    • Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1
    • T. Yoshida M. Yohda T. Iida T. Maruyama H. Taguchi K. Yazaki Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1 J. Mol. Biol. 273 1997 635 645
    • (1997) J. Mol. Biol. , vol.273 , pp. 635-645
    • Yoshida, T.1    Yohda, M.2    Iida, T.3    Maruyama, T.4    Taguchi, H.5    Yazaki, K.6
  • 17
    • 0034705345 scopus 로고    scopus 로고
    • Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1 [Corrigendum]
    • T. Yoshida M. Yohda T. Iida T. Maruyama H. Taguchi K. Yazaki Structural and functional characterization of homo-oligomeric complexes of alpha and beta chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1 [Corrigendum] J. Mol. Biol. 299 2000 1399 1400
    • (2000) J. Mol. Biol. , vol.299 , pp. 1399-1400
    • Yoshida, T.1    Yohda, M.2    Iida, T.3    Maruyama, T.4    Taguchi, H.5    Yazaki, K.6
  • 18
    • 0036290267 scopus 로고    scopus 로고
    • Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin
    • T. Yoshida R. Kawaguchi H. Taguchi M. Yoshida T. Yasunaga T. Wakabayashi Archaeal group II chaperonin mediates protein folding in the cis -cavity without a detachable GroES-like co-chaperonin J. Mol. Biol. 315 2002 73 85
    • (2002) J. Mol. Biol. , vol.315 , pp. 73-85
    • Yoshida, T.1    Kawaguchi, R.2    Taguchi, H.3    Yoshida, M.4    Yasunaga, T.5    Wakabayashi, T.6
  • 19
    • 21244434862 scopus 로고    scopus 로고
    • Facilitated release of substrate protein from prefoldin by chaperonin
    • T. Zako R. Iizuka M. Okochi T. Nomura T. Ueno H. Tadakuma Facilitated release of substrate protein from prefoldin by chaperonin FEBS Lett. 579 2005 3718 3724
    • (2005) FEBS Lett. , vol.579 , pp. 3718-3724
    • Zako, T.1    Iizuka, R.2    Okochi, M.3    Nomura, T.4    Ueno, T.5    Tadakuma, H.6
  • 20
    • 33750287973 scopus 로고    scopus 로고
    • Localization of prefoldin interaction sites in the hyperthermophilic group II chaperonin and correlations between binding rate and protein transfer rate
    • T. Zako Y. Murase R. Iizuka T. Yoshida T. Kanzaki N. Ide Localization of prefoldin interaction sites in the hyperthermophilic group II chaperonin and correlations between binding rate and protein transfer rate J. Mol. Biol. 364 2006 110 120
    • (2006) J. Mol. Biol. , vol.364 , pp. 110-120
    • Zako, T.1    Murase, Y.2    Iizuka, R.3    Yoshida, T.4    Kanzaki, T.5    Ide, N.6
  • 21
    • 13544250517 scopus 로고    scopus 로고
    • Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes
    • T. Fukui H. Atomi T. Kanai R. Matsumi S. Fujiwara T. Imanaka Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes Genome Res. 15 2005 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
  • 22
    • 33947720464 scopus 로고    scopus 로고
    • A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii
    • T.A. Whitehead B.B. Boonyaratanakornkit V. Hollrigl D.S. Clark A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii Protein Sci. 16 2007 626 634
    • (2007) Protein Sci. , vol.16 , pp. 626-634
    • Whitehead, T.A.1    Boonyaratanakornkit, B.B.2    Hollrigl, V.3    Clark, D.S.4
  • 23
    • 0027498262 scopus 로고
    • Light-scattering and the absolute characterization of macromolecules
    • P.J. Wyatt Light-scattering and the absolute characterization of macromolecules Anal. Chim. Acta 272 1993 1 40
    • (1993) Anal. Chim. Acta , vol.272 , pp. 1-40
    • Wyatt, P.J.1
  • 24
    • 39049170168 scopus 로고    scopus 로고
    • Structure and molecular dynamics simulation of archaeal prefoldin: the molecular mechanism for binding and recognition of nonnative substrate Proteins
    • A. Ohtaki H. Kida Y. Miyata N. Ide A. Yonezawa T. Arakawa Structure and molecular dynamics simulation of archaeal prefoldin: the molecular mechanism for binding and recognition of nonnative substrate Proteins J Mol Biol. 376 2008 1130 1141
    • (2008) J Mol Biol. , vol.376 , pp. 1130-1141
    • Ohtaki, A.1    Kida, H.2    Miyata, Y.3    Ide, N.4    Yonezawa, A.5    Arakawa, T.6
  • 25
    • 0034812522 scopus 로고    scopus 로고
    • Two kinds of archaeal chaperonin with different temperature dependency from a hyperthermophile
    • M. Izumi S. Fujiwara M. Takagi K. Fukui T. Imanaka Two kinds of archaeal chaperonin with different temperature dependency from a hyperthermophile Biochem. Biophys. Res. Commun. 280 2001 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
  • 26
    • 0035107355 scopus 로고    scopus 로고
    • Natural chaperonin of the hyperthermophilic archaeum, Thermococcus strain KS-1: a hetero-oligomeric chaperonin with variable subunit composition
    • T. Yoshida A. Ideno S. Hiyamuta M. Yohda T. Maruyama Natural chaperonin of the hyperthermophilic archaeum, Thermococcus strain KS-1: a hetero-oligomeric chaperonin with variable subunit composition Mol. Microbiol. 39 2001 1406 1413
    • (2001) Mol. Microbiol. , vol.39 , pp. 1406-1413
    • Yoshida, T.1    Ideno, A.2    Hiyamuta, S.3    Yohda, M.4    Maruyama, T.5
  • 27
    • 18944394260 scopus 로고    scopus 로고
    • Transcriptional profiling of the hyperthermophilic methanarchaeon Methanococcus jannaschii in response to lethal heat and non-lethal cold shock
    • B.B. Boonyaratanakornkit A.J. Simpson T.A. Whitehead C.M. Fraser N.M. El-Sayed D.S. Clark Transcriptional profiling of the hyperthermophilic methanarchaeon Methanococcus jannaschii in response to lethal heat and non-lethal cold shock Environ. Microbiol. 7 2005 789 797
    • (2005) Environ. Microbiol. , vol.7 , pp. 789-797
    • Boonyaratanakornkit, B.B.1    Simpson, A.J.2    Whitehead, T.A.3    Fraser, C.M.4    El-Sayed, N.M.5    Clark, D.S.6
  • 28
    • 0032579989 scopus 로고    scopus 로고
    • Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3
    • Y. Kawarabayasi M. Sawada H. Horikawa Y. Haikawa Y. Hino S. Yamamoto Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3 DNA Res. 5 1998 55 76
    • (1998) DNA Res. , vol.5 , pp. 55-76
    • Kawarabayasi, Y.1    Sawada, M.2    Horikawa, H.3    Haikawa, Y.4    Hino, Y.5    Yamamoto, S.6
  • 29
    • 0037346631 scopus 로고    scopus 로고
    • An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi
    • G.N. Cohen V. Barbe D. Flament M. Galperin R. Heilig O. Lecompte An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi Mol. Microbiol. 47 2003 1495 1512
    • (2003) Mol. Microbiol. , vol.47 , pp. 1495-1512
    • Cohen, G.N.1    Barbe, V.2    Flament, D.3    Galperin, M.4    Heilig, R.5    Lecompte, O.6
  • 30
    • 0035142375 scopus 로고    scopus 로고
    • Genomic sequence of hyperthermophile, Pyrococcus furiosus: implications for physiology and enzymology
    • F.T. Robb D.L. Maeder J.R. Brown J. DiRuggiero M.D. Stump R.K. Yeh Genomic sequence of hyperthermophile, Pyrococcus furiosus : implications for physiology and enzymology Methods Enzymol. 330 2001 134 157
    • (2001) Methods Enzymol. , vol.330 , pp. 134-157
    • Robb, F.T.1    Maeder, D.L.2    Brown, J.R.3    DiRuggiero, J.4    Stump, M.D.5    Yeh, R.K.6
  • 31
    • 0033598189 scopus 로고    scopus 로고
    • Recurrent paralogy in the evolution of archaeal chaperonins
    • J.M. Archibald J.M. Logsdon W.F. Doolittle Recurrent paralogy in the evolution of archaeal chaperonins Curr. Biol. 9 1999 1053 1056
    • (1999) Curr. Biol. , vol.9 , pp. 1053-1056
    • Archibald, J.M.1    Logsdon, J.M.2    Doolittle, W.F.3
  • 32
    • 0141957432 scopus 로고    scopus 로고
    • Taxonomy of nonmethanogenic hyperthermophilic and related thermophilic archaea
    • T. Itoh Taxonomy of nonmethanogenic hyperthermophilic and related thermophilic archaea J. Biosci. Bioeng. 96 2003 203 212
    • (2003) J. Biosci. Bioeng. , vol.96 , pp. 203-212
    • Itoh, T.1
  • 33
    • 0028989757 scopus 로고
    • Dense community of hyperthermophilic sulfur-dependent heterotrophs in a geothermally heated shallow submarine biotope near Kodakara–Jima Island, Kagoshima, Japan
    • T. Hoaki M. Nishijima H. Miyashita T. Maruyama Dense community of hyperthermophilic sulfur-dependent heterotrophs in a geothermally heated shallow submarine biotope near Kodakara–Jima Island, Kagoshima, Japan Appl. Environ. Microbiol. 61 1995 1931 1937
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1931-1937
    • Hoaki, T.1    Nishijima, M.2    Miyashita, H.3    Maruyama, T.4
  • 34
    • 28844440537 scopus 로고    scopus 로고
    • Characterization of archaeal group II chaperonin–ADP–metal fluoride complexes: implications that group II chaperonins operate as a “two-stroke engine”
    • R. Iizuka T. Yoshida N. Ishii T. Zako K. Takahashi K. Maki Characterization of archaeal group II chaperonin–ADP–metal fluoride complexes: implications that group II chaperonins operate as a “two-stroke engine” J. Biol. Chem. 280 2005 40375 40383
    • (2005) J. Biol. Chem. , vol.280 , pp. 40375-40383
    • Iizuka, R.1    Yoshida, T.2    Ishii, N.3    Zako, T.4    Takahashi, K.5    Maki, K.6
  • 35
    • 0032788447 scopus 로고    scopus 로고
    • Circularly permuted variants of the green fluorescent protein
    • S. Topell J. Hennecke R. Glockshuber Circularly permuted variants of the green fluorescent protein FEBS Lett. 457 1999 283 289
    • (1999) FEBS Lett. , vol.457 , pp. 283-289
    • Topell, S.1    Hennecke, J.2    Glockshuber, R.3
  • 36
    • 0035930935 scopus 로고    scopus 로고
    • Glycine at the 65th position plays an essential role in ATP-dependent protein folding by Archael group II chaperonin
    • R. Iizuka T. Yoshida T. Maruyama Y. Shomura K. Miki M. Yohda Glycine at the 65th position plays an essential role in ATP-dependent protein folding by Archael group II chaperonin Biochem. Biophys. Res. Commun. 289 2001 1118 1124
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 1118-1124
    • Iizuka, R.1    Yoshida, T.2    Maruyama, T.3    Shomura, Y.4    Miki, K.5    Yohda, M.6
  • 37
    • 0242581721 scopus 로고    scopus 로고
    • ATP binding is critical for the conformational change from an open to closed state in archaeal group II chaperonin
    • R. Iizuka T. Yoshida Y. Shomura K. Miki T. Maruyama M. Odaka M. Yohda ATP binding is critical for the conformational change from an open to closed state in archaeal group II chaperonin J. Biol. Chem. 278 2003 44959 44965
    • (2003) J. Biol. Chem. , vol.278 , pp. 44959-44965
    • Iizuka, R.1    Yoshida, T.2    Shomura, Y.3    Miki, K.4    Maruyama, T.5    Odaka, M.6    Yohda, M.7


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