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Volumn 10, Issue 6, 2006, Pages 537-549

Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps

Author keywords

Antarctic fish; CCT; Chaperonin; Cofactor A; cpn60; Protein folding; Tubulin

Indexed keywords

CHAPERONIN; CYTOSKELETON PROTEIN; FISH PROTEIN; PROTEIN SUBUNIT; T COMPLEX POLYPEPTIDE 1; T-COMPLEX POLYPEPTIDE-1; TUBULIN;

EID: 33751088510     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-006-0528-x     Document Type: Article
Times cited : (18)

References (54)
  • 1
    • 0037424811 scopus 로고    scopus 로고
    • Structural characterization of En-1, a cold-adapted protein pheromone isolated from the Antarctic ciliate Euplotes nobilii
    • Alimenti C, Ortenzi C, Carratore V, Luporini P (2003) Structural characterization of En-1, a cold-adapted protein pheromone isolated from the Antarctic ciliate Euplotes nobilii. Biochimica Biophysica Acta 1621:17-21
    • (2003) Biochimica Biophysica Acta , vol.1621 , pp. 17-21
    • Alimenti, C.1    Ortenzi, C.2    Carratore, V.3    Luporini, P.4
  • 3
    • 0034711208 scopus 로고    scopus 로고
    • Cold adaptation of microtubule assembly and dynamics: Structural interpretation of primary Sequence changes present in the α- and β-tubulins of Antarctic fishes
    • Detrich HW, Parker SK, Williams RC, Nogales E, Downing KH (2000) Cold adaptation of microtubule assembly and dynamics: structural interpretation of primary Sequence changes present in the α- and β-tubulins of Antarctic fishes. J. Biol Che. 275:37038-37048
    • (2000) J. Biol Che. , vol.275 , pp. 37038-37048
    • Detrich, H.W.1    Parker, S.K.2    Williams, R.C.3    Nogales, E.4    Downing, K.H.5
  • 4
    • 0002392493 scopus 로고
    • Coastal and deep-water benthic fishes of the Antarctic
    • Bushnell VC (ed) Folio 15. American Geographical Society, New York
    • DeWitt HH (1971) Coastal and deep-water benthic fishes of the Antarctic. In: Bushnell VC (ed) Antarctic Map Folio Series, Folio 15. American Geographical Society, New York, pp 1-10
    • (1971) Antarctic Map Folio Series , pp. 1-10
    • DeWitt, H.H.1
  • 7
    • 0030681366 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Molecular basis of cold adaptation
    • Feller G, Gerday C (1997) Psychrophilic enzymes: molecular basis of cold adaptation. Cell Mol Life Sci 53:830-841
    • (1997) Cell Mol Life Sci , vol.53 , pp. 830-841
    • Feller, G.1    Gerday, C.2
  • 8
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: Localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes
    • Fields PA, Somero GN (1998) Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes. Procl Natl Acad Sci USA 95:11476-11481
    • (1998) Procl Natl Acad Sci USA , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 9
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman J, Nimmesgern E, Erdjument-Bromage H, Wall JS, Tempst P, Hartl FU (1992) Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J 11:4767-4778
    • (1992) EMBO J , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.U.6
  • 10
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta actin folding
    • Gao Y, Thomas JO, Chow RL, Lee GH, Cowan NJ (1992) A cytoplasmic chaperonin that catalyzes beta actin folding. Cell 69:1044-1050
    • (1992) Cell , vol.69 , pp. 1044-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 11
    • 0027528871 scopus 로고
    • Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin
    • Gao Y, Vainberg IE, Chow RL, Cowan NJ (1993) Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin. Mol Cell Biol 13:2488-2485
    • (1993) Mol Cell Biol , vol.13 , pp. 2488-12485
    • Gao, Y.1    Vainberg, I.E.2    Chow, R.L.3    Cowan, N.J.4
  • 13
    • 0032491412 scopus 로고    scopus 로고
    • The chaperone cofactor Hop/p60 interacts with the cytosolyc chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities
    • Gebauer M, Melki R, Gehring U (1998) The chaperone cofactor Hop/p60 interacts with the cytosolyc chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities. J Biol Chem 273:29475-29480
    • (1998) J Biol Chem , vol.273 , pp. 29475-29480
    • Gebauer, M.1    Melki, R.2    Gehring, U.3
  • 14
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional alpha and gamma-tubulin
    • Geissler S, Siegers K, Schiebel E (1998) A novel protein complex promoting formation of functional alpha and gamma-tubulin. EMBO J 17:952-966
    • (1998) EMBO J , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 15
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb-Viewer: An environment for comparative protein modelling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-Pdb-Viewer: An environment for comparative protein modelling. Electrophoresis 18:2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 16
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 17
    • 0020985843 scopus 로고
    • A comparative study of protein synthesis in nototheniids and icefish at Palmer Station, Antarctica
    • Haschemeyer AEV (1983) A comparative study of protein synthesis in nototheniids and icefish at Palmer Station, Antarctica. Comp Biochem Physiol B 76:541-543
    • (1983) Comp Biochem Physiol B , vol.76 , pp. 541-543
    • Haschemeyer, A.E.V.1
  • 18
    • 0033067705 scopus 로고    scopus 로고
    • WinGene/WinPep: User-friendly software for the analysis of aminoacid sequences
    • Hennig L (1999) WinGene/WinPep: user-friendly software for the analysis of aminoacid sequences. BioTechniques 26:1170-1172
    • (1999) BioTechniques , vol.26 , pp. 1170-1172
    • Hennig, L.1
  • 19
    • 0029062216 scopus 로고
    • Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
    • Kubota H, Hynes G, Willison K (1995) Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur J Biochem 230:3-16
    • (1995) Eur J Biochem , vol.230 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 20
    • 0035929150 scopus 로고    scopus 로고
    • Chaperonins-keeping a lid on folding proteins
    • Kusmierczyk AR, Martin J (2001) Chaperonins-keeping a lid on folding proteins. FEBS Lett 505:343-347
    • (2001) FEBS Lett , vol.505 , pp. 343-347
    • Kusmierczyk, A.R.1    Martin, J.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 15:680-685
    • (1970) Nature , vol.15 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0035831272 scopus 로고    scopus 로고
    • High macromolecular synthesis with low metabolic cost in Antarctic sea urchin embryos
    • Marsh AG, Maxson RE Jr, Manahan DT (2001) High macromolecular synthesis with low metabolic cost in Antarctic sea urchin embryos. Science 291:1950-1952
    • (2001) Science , vol.291 , pp. 1950-1952
    • Marsh, A.G.1    Maxson Jr., R.E.2    Manahan, D.T.3
  • 29
    • 0035783387 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes of the chaperonin containing tcp-1
    • Melki R (2001) Nucleotide-dependent conformational changes of the chaperonin containing tcp-1. J Struct Biol 135:170-175
    • (2001) J Struct Biol , vol.135 , pp. 170-175
    • Melki, R.1
  • 30
    • 0028196813 scopus 로고
    • Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
    • Melki R, Cowan NJ (1994) Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates. Mol Cell Biol. 14:2895-2904
    • (1994) Mol Cell Biol. , vol.14 , pp. 2895-2904
    • Melki, R.1    Cowan, N.J.2
  • 31
    • 0025146397 scopus 로고
    • Direct evidence for GTP and GDP-Pi intermediates in microtubule assembly
    • Melki R, Carlier MF, Pantaloni D (1990) Direct evidence for GTP and GDP-Pi intermediates in microtubule assembly. Biochemistry 29:8921-8932
    • (1990) Biochemistry , vol.29 , pp. 8921-8932
    • Melki, R.1    Carlier, M.F.2    Pantaloni, D.3
  • 32
    • 0029848951 scopus 로고    scopus 로고
    • Cofactor A is a molecular chaperone required for beta-tubulin folding: Functional and structural characterization
    • Melki R, Rommelaere H, Leguy R, Vandekerckhove J, Ampe C (1996) Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization. Biochemistry 35:10432-10445
    • (1996) Biochemistry , vol.35 , pp. 10432-10445
    • Melki, R.1    Rommelaere, H.2    Leguy, R.3    Vandekerckhove, J.4    Ampe, C.5
  • 33
    • 0343907201 scopus 로고    scopus 로고
    • Cytoplasmic chaperonin containing TCP-1: Structural and functional characterization
    • Melki R, Batelier G, Soulie S, Williams Jr RC (1997) Cytoplasmic chaperonin containing TCP-1: structural and functional characterization. Biochemistry 36:5817-5826
    • (1997) Biochemistry , vol.36 , pp. 5817-5826
    • Melki, R.1    Batelier, G.2    Soulie, S.3    Williams Jr., R.C.4
  • 34
    • 2942559297 scopus 로고    scopus 로고
    • NRC (National Research Council) National Academy Press, Washington
    • NRC (National Research Council) (2003) Frontiers in polar biology in the genomic era. National Academy Press, Washington
    • (2003) Frontiers in Polar Biology in the Genomic Era
  • 35
    • 0035983515 scopus 로고    scopus 로고
    • Crystal structure of the CCTgamma apical domain: Implications for substrate binding to the eukaryotic cytosolic chaperonin
    • Pappenberger G, Wilsher JA, Roe SM, Counsell DJ, Willison KR, Pearl LH (2002) Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. J Mol. Biol. 318:1367-1379
    • (2002) J Mol. Biol. , vol.318 , pp. 1367-1379
    • Pappenberger, G.1    Wilsher, J.A.2    Roe, S.M.3    Counsell, D.J.4    Willison, K.R.5    Pearl, L.H.6
  • 37
    • 0029004590 scopus 로고
    • Protein modeling by E-mail
    • Peitsch MC (1995) Protein modeling by E-mail. Biotechnology 13:658-660
    • (1995) Biotechnology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 38
    • 16444385033 scopus 로고    scopus 로고
    • Constitutive expression of a stress-inducible heat shock protein gene, hsp70, in phylogenetically distant Antarctic fish
    • Place SP, Hofmann GE (2005) Constitutive expression of a stress-inducible heat shock protein gene, hsp70, in phylogenetically distant Antarctic fish. Pol Biol 28:261-267
    • (2005) Pol Biol , vol.28 , pp. 261-267
    • Place, S.P.1    Hofmann, G.E.2
  • 39
    • 3242769102 scopus 로고    scopus 로고
    • Comparison of Hsc70 orthologues from polar and temperate notothenioid fishes: Differences in the prevention of aggregation and refolding of denatured proteins Am
    • Place SP, Zippay ML, Hofmann GE (2004) Comparison of Hsc70 orthologues from polar and temperate notothenioid fishes: differences in the prevention of aggregation and refolding of denatured proteins Am. J Physiol Regul Integr Comp Physiol 287:R429-R436
    • (2004) J Physiol Regul Integr Comp Physiol , vol.287
    • Place, S.P.1    Zippay, M.L.2    Hofmann, G.E.3
  • 41
    • 0030772842 scopus 로고    scopus 로고
    • Cold-adapted microtubules: Characterization of tubulin posttranslational modifications in the Antarctic ciliate Euplotes focardii
    • Pucciarelli S, Ballarini P, Miceli C (1997) Cold-adapted microtubules: characterization of tubulin posttranslational modifications in the Antarctic ciliate Euplotes focardii. Cell Motil Cytoskeleton 38:329-341
    • (1997) Cell Motil Cytoskeleton , vol.38 , pp. 329-341
    • Pucciarelli, S.1    Ballarini, P.2    Miceli, C.3
  • 42
    • 0036451228 scopus 로고    scopus 로고
    • Heterologous expression and folding analysis of a beta-tubulin isotype from the Antarctic ciliate Euplotes focardii
    • Pucciarelli S, Miceli C, Melki R (2002) Heterologous expression and folding analysis of a beta-tubulin isotype from the Antarctic ciliate Euplotes focardii. Eur J Biochem 269:6271-6277
    • (2002) Eur J Biochem , vol.269 , pp. 6271-6277
    • Pucciarelli, S.1    Miceli, C.2    Melki, R.3
  • 43
    • 26844555780 scopus 로고    scopus 로고
    • Ribosomal cold-adaptation: Characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii
    • Pucciarelli S, Marziale F, Di Giuseppe G, Barchetta S, Miceli C (2005) Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii. Gene 360(2):103-110
    • (2005) Gene , vol.360 , Issue.2 , pp. 103-110
    • Pucciarelli, S.1    Marziale, F.2    Di Giuseppe, G.3    Barchetta, S.4    Miceli, C.5
  • 44
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31:3381-3385
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 45
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I (2000) Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell. 103(4):621-632
    • (2000) Cell , vol.103 , Issue.4 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 46
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • Spiess C, Meyer AS, Reissmann S, Frydman J (2004) Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol 14:598-604
    • (2004) Trends Cell Biol , vol.14 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 47
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford WF III (1992) Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal Biochem. 203:295-301
    • (1992) Anal Biochem. , vol.203 , pp. 295-301
    • Stafford III, W.F.1
  • 49
    • 0020359569 scopus 로고
    • Polymerization thermodynamics and structural stabilities of skeletal muscle actins from vertebrates adapted to different temperatures and hydrostatic pressures
    • Swezey RR, Somero GN (1982) Polymerization thermodynamics and structural stabilities of skeletal muscle actins from vertebrates adapted to different temperatures and hydrostatic pressures. Biochemistry 21:4496-4503
    • (1982) Biochemistry , vol.21 , pp. 4496-4503
    • Swezey, R.R.1    Somero, G.N.2
  • 50
    • 0033588020 scopus 로고    scopus 로고
    • Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the α/β tubulin heterodimer
    • Tian G, Bhamidipati A, Cowan NJ, Lewis SA (1999) Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the α/β tubulin heterodimer. J Biol Chem 274:24154-24158
    • (1999) J Biol Chem , vol.274 , pp. 24154-24158
    • Tian, G.1    Bhamidipati, A.2    Cowan, N.J.3    Lewis, S.A.4
  • 54
    • 0034644667 scopus 로고    scopus 로고
    • Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution
    • Wintrode PL, Miyazaki K, Arnold FH (2000) Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution J. Biol Chem 275:31635-31640
    • (2000) J. Biol Chem , vol.275 , pp. 31635-31640
    • Wintrode, P.L.1    Miyazaki, K.2    Arnold, F.H.3


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