메뉴 건너뛰기




Volumn 107, Issue 11, 2010, Pages 4967-4972

4.0-Å resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement

Author keywords

Asymmetric reconstruction; Atomic model; Subunit structure

Indexed keywords

CHAPERONIN; OLIGOMER; PROTEOME; CHAPERONIN CONTAINING TCP1; PROTEIN SUBUNIT;

EID: 77950456761     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0913774107     Document Type: Article
Times cited : (136)

References (48)
  • 1
    • 1542675962 scopus 로고    scopus 로고
    • Aberrant protein folding as the molecular basis of cancer
    • Scott MD, Frydman J (2003) Aberrant protein folding as the molecular basis of cancer. Method Mol Biol 232:67-76.
    • (2003) Method Mol Biol , vol.232 , pp. 67-76
    • Scott, M.D.1    Frydman, J.2
  • 2
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto RI (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev 22:1427-1438.
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 3
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • DOI 10.1016/j.semcdb.2003.12.008
    • Dobson CM (2004) Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol 15:3-16. (Pubitemid 38177363)
    • (2004) Seminars in Cell and Developmental Biology , vol.15 , Issue.1 , pp. 3-16
    • Dobson, C.M.1
  • 4
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J (2001) Folding of newly translated proteins in vivo: The role of molecular chaperones. Annu Rev Biochem 70:603-647.
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 5
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, 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
  • 8
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • DOI 10.1038/ncb1477, PII NCB1477
    • Tam S, Geller R, Spiess C, Frydman J (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8:1155-1162. (Pubitemid 44473612)
    • (2006) Nature Cell Biology , vol.8 , Issue.10 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 9
    • 0035783192 scopus 로고    scopus 로고
    • Review: Cellular substrates of the eukaryotic chaperonin TRiC/CCT
    • DOI 10.1006/jsbi.2001.4380
    • Dunn AY, Melville MW, Frydman J (2001) Review: Cellular substrates of the eukaryotic chaperonin TRiC/CCT. J Struct Biol 135:176-184. (Pubitemid 33733506)
    • (2001) Journal of Structural Biology , vol.135 , Issue.2 , pp. 176-184
    • Dunn, A.Y.1    Melville, M.W.2    Frydman, J.3
  • 10
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • Yam AY, et al. (2008) Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat Struct Mol Biol 15:1255-1262.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1255-1262
    • Yam, A.Y.1
  • 11
    • 0034611628 scopus 로고    scopus 로고
    • Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT
    • Leroux MR, Hartl FU (2000) Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT. Curr Biol 10:R260-264.
    • (2000) Curr Biol , vol.10
    • Leroux, M.R.1    Hartl, F.U.2
  • 12
    • 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 AS, Reissmann S, 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
  • 13
    • 46449109112 scopus 로고    scopus 로고
    • Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT
    • Booth CR, et al. (2008) Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nat Struct Mol Biol 15:746-753.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 746-753
    • Booth, C.R.1
  • 14
    • 0038737003 scopus 로고    scopus 로고
    • Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
    • Meyer AS, et al. (2003) Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113:369-381.
    • (2003) Cell , vol.113 , pp. 369-381
    • Meyer, A.S.1
  • 15
    • 34247635168 scopus 로고    scopus 로고
    • Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins
    • DOI 10.1038/nsmb1236, PII NSMB1236
    • Reissmann S, Parnot C, Booth CR, Chiu W, Frydman J (2007) Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins. Nat Struct Mol Biol 14:432-440. (Pubitemid 46685886)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.5 , pp. 432-440
    • Reissmann, S.1    Parnot, C.2    Booth, C.R.3    Chiu, W.4    Frydman, J.5
  • 16
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
    • Gutsche I, Essen LO, BaumeisterW(1999) Group II chaperonins: New TRiC(k)s and turns of a protein folding machine. J Mol Biol 293:295-312.
    • (1999) J Mol Biol , vol.293 , pp. 295-312
    • Gutsche, I.1    Essen, L.O.2    Baumeister, W.3
  • 17
    • 0035783161 scopus 로고    scopus 로고
    • Gene duplication and the evolution of group II chaperonins: Implications for structure and function
    • DOI 10.1006/jsbi.2001.4353
    • Archibald JM, Blouin C, Doolittle WF (2001) Gene duplication and the evolution of group II chaperonins: Implications for structure and function. J Struct Biol 135:157-169. (Pubitemid 33733504)
    • (2001) Journal of Structural Biology , vol.135 , Issue.2 , pp. 157-169
    • Archibald, J.M.1    Blouin, C.2    Doolittle, W.F.3
  • 18
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • DOI 10.1038/41944
    • Xu Z, Horwich AL, Sigler PB (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388:741-750. (Pubitemid 27375147)
    • (1997) Nature , vol.388 , Issue.6644 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 19
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • DOI 10.1016/S0092-8674(00)81152-6
    • Ditzel L, et al. (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93:125-138. (Pubitemid 28173558)
    • (1998) Cell , vol.93 , Issue.1 , 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
  • 21
    • 0037010171 scopus 로고    scopus 로고
    • Structure and function of a protein folding machine: The eukaryotic cytosolic chaperonin CCT
    • DOI 10.1016/S0014-5793(02)03180-0, PII S0014579302031800
    • Valpuesta JM, Martin-Benito J, Gomez-Puertas P, Carrascosa JL, Willison KR (2002) Structure and function of a protein folding machine: The eukaryotic cytosolic chaperonin CCT. FEBS Lett 529:11-16. (Pubitemid 35283904)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 11-16
    • Valpuesta, J.M.1    Martin-Benito, J.2    Gomez-Puertas, P.3    Carrascosa, J.L.4    Willison, K.R.5
  • 22
    • 23044445800 scopus 로고    scopus 로고
    • The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking
    • Etchells SA, et al. (2005) The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking. J Biol Chem 280:28118-28126.
    • (2005) J Biol Chem , vol.280 , pp. 28118-28126
    • Etchells, S.A.1
  • 23
    • 33749080319 scopus 로고    scopus 로고
    • Identification of the TRiC/CCT Substrate Binding Sites Uncovers the Function of Subunit Diversity in Eukaryotic Chaperonins
    • DOI 10.1016/j.molcel.2006.09.003, PII S1097276506006319
    • Spiess C, Miller EJ, McClellan AJ, Frydman J (2006) Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell 24:25-37. (Pubitemid 44466686)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 25-37
    • Spiess, C.1    Miller, E.J.2    McClellan, A.J.3    Frydman, J.4
  • 24
    • 0030842428 scopus 로고    scopus 로고
    • Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes
    • Liou AK, Willison KR (1997) Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes. EMBO J 16:4311-4316.
    • (1997) EMBO J , vol.16 , pp. 4311-4316
    • Liou, A.K.1    Willison, K.R.2
  • 25
    • 0035423032 scopus 로고    scopus 로고
    • The "sequential allosteric ring" mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin
    • Llorca O, et al. (2001) The "sequential allosteric ring" mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin. EMBO J 20:4065-4075.
    • (2001) EMBO J , vol.20 , pp. 4065-4075
    • Llorca, O.1
  • 27
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128:82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 28
    • 40049105503 scopus 로고    scopus 로고
    • De novo backbone trace of GroEL from single particle electron cryomicroscopy
    • Ludtke SJ, et al. (2008) De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure 16:441-448.
    • (2008) Structure , vol.16 , pp. 441-448
    • Ludtke, S.J.1
  • 29
    • 2442592916 scopus 로고    scopus 로고
    • Role of the Helical Protrusion in the Conformational Change and Molecular Chaperone Activity of the Archaeal Group II Chaperonin
    • DOI 10.1074/jbc.M400839200
    • Iizuka R, et al. (2004) Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin. J Biol Chem 279:18834-18839. (Pubitemid 38623310)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18834-18839
    • Iizuka, R.1    So, S.2    Inobe, T.3    Yoshida, T.4    Zako, T.5    Kuwajima, K.6    Yohda, M.7
  • 30
    • 42649124830 scopus 로고    scopus 로고
    • Protein interactions captured by chemical cross-linking
    • ed Golemis EA (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York), 2nd Ed
    • Nadeau OW, Carlson GM (2005) Protein interactions captured by chemical cross-linking. Protein-Protein Interactions: A Molecular Cloning Manual, ed Golemis EA (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York), 2nd Ed, pp 105-128.
    • (2005) Protein-Protein Interactions: A Molecular Cloning Manual , pp. 105-128
    • Nadeau, O.W.1    Carlson, G.M.2
  • 33
    • 68949187842 scopus 로고    scopus 로고
    • Refinement of protein structures into low-resolution density maps using rosetta
    • DiMaio F, Tyka MD, Baker ML, Chiu W, Baker D (2009) Refinement of protein structures into low-resolution density maps using rosetta. J Mol Biol 392:181-190.
    • (2009) J Mol Biol , vol.392 , pp. 181-190
    • DiMaio, F.1    Tyka, M.D.2    Baker, M.L.3    Chiu, W.4    Baker, D.5
  • 35
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang G, et al. (2007) EMAN2: An extensible image processing suite for electron microscopy. J Struct Biol 157:38-46.
    • (2007) J Struct Biol , vol.157 , pp. 38-46
    • Tang, G.1
  • 36
    • 0344552370 scopus 로고    scopus 로고
    • 2D fast rotational matching for image processing of biophysical data
    • DOI 10.1016/j.jsb.2003.09.017
    • Cong Y, Kovacs JA, Wriggers W (2003) 2D fast rotational matching for image processing of biophysical data. J Struct Biol 144:51-60. (Pubitemid 37468366)
    • (2003) Journal of Structural Biology , vol.144 , Issue.1-2 , pp. 51-60
    • Cong, Y.1    Kovacs, J.A.2    Wriggers, W.3
  • 38
    • 33744454409 scopus 로고    scopus 로고
    • Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiC
    • Miller EJ, Meyer AS, Frydman J (2006) Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiC. Protein Sci 15:1522-1526.
    • (2006) Protein Sci , vol.15 , pp. 1522-1526
    • Miller, E.J.1    Meyer, A.S.2    Frydman, J.3
  • 39
    • 17844378217 scopus 로고    scopus 로고
    • Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
    • DOI 10.1038/nsmb901
    • Rivenzon-Segal D, Wolf SG, Shimon L, Willison KR, Horovitz A (2005) Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat Struct Mol Biol 12:233-237. (Pubitemid 43079364)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.3 , pp. 233-237
    • Rivenzon-Segal, D.1    Wolf, S.G.2    Shimon, L.3    Willison, K.R.4    Horovitz, A.5
  • 40
    • 33646897305 scopus 로고    scopus 로고
    • Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
    • Tang YC, et al. (2006) Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 125:903-914.
    • (2006) Cell , vol.125 , pp. 903-914
    • Tang, Y.C.1
  • 42
    • 0034572910 scopus 로고    scopus 로고
    • Purification of the cytosolic chaperonin TRiC from bovine testis
    • Ferreyra RG, Frydman J (2000) Purification of the cytosolic chaperonin TRiC from bovine testis. Method Mol Biol 140:153-160.
    • (2000) Method Mol Biol , vol.140 , pp. 153-160
    • Ferreyra, R.G.1    Frydman, J.2
  • 44
    • 65149093437 scopus 로고    scopus 로고
    • Structural mechanism of SDS-induced enzyme activity of scorpion hemocyanin revealed by electron cryomicroscopy
    • Cong Y, et al. (2009) Structural mechanism of SDS-induced enzyme activity of scorpion hemocyanin revealed by electron cryomicroscopy. Structure 17:749-758.
    • (2009) Structure , vol.17 , pp. 749-758
    • Cong, Y.1
  • 45
    • 0000313739 scopus 로고
    • Exact filters for general geometry three dimensional reconstruction
    • Harauz G, van Heel M (1986) Exact filters for general geometry three dimensional reconstruction. Optik 73:146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    Van Heel, M.2
  • 46
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333:721-745.
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 47
    • 51549084591 scopus 로고    scopus 로고
    • Sharpening high resolution information in single particle electron cryomicroscopy
    • Fernandez JJ, Luque D, Caston JR, Carrascosa JL (2008) Sharpening high resolution information in single particle electron cryomicroscopy. J Struct Biol 164:170-175.
    • (2008) J Struct Biol , vol.164 , pp. 170-175
    • Fernandez, J.J.1    Luque, D.2    Caston, J.R.3    Carrascosa, J.L.4
  • 48
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, et al. (2007) MolProbity: All-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35:W375-383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.