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Volumn 66, Issue , 2000, Pages 41-66

Folding of a nascent peptide on the ribosome

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DNAK PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; GRPE PROTEIN, BACTERIA; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; PEPTIDE; RNA;

EID: 0035193534     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0079-6603(00)66026-9     Document Type: Review
Times cited : (97)

References (85)
  • 2
    • 0031803521 scopus 로고    scopus 로고
    • The three-dimensional structure of the ribosome and its components
    • P.B Moore The three-dimensional structure of the ribosome and its components Annu. Rev. Biophys. Biomol. Struct. 27 1998 35 38
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 35-38
    • Moore, P.B1
  • 4
    • 0033117764 scopus 로고    scopus 로고
    • Structural studies of the translational apparatus
    • R.K Agrawal J Frank Structural studies of the translational apparatus Curr. Opin. Struct. Biol. 9 1999 215 221
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 215-221
    • Agrawal, R.K1    Frank, J2
  • 5
    • 0033000020 scopus 로고    scopus 로고
    • Structural information for explaining the molecular mechanism of protein biosynthesis
    • B.F Clark S Thirup M Kjeldgaard J Nyborg Structural information for explaining the molecular mechanism of protein biosynthesis FEBS Lett. 452 1999 41 46
    • (1999) FEBS Lett. , vol.452 , pp. 41-46
    • Clark, B.F1    Thirup, S2    Kjeldgaard, M3    Nyborg, J4
  • 6
    • 85119559523 scopus 로고    scopus 로고
    • R Garrett S Douthwaite A Liljas A Matheson P Moore H Noller The Ribosome: Structure, Function, Antibiotics and Cellular Interactions 2000 ASM Press Washington, D.C
    • (2000)
  • 7
    • 0000927677 scopus 로고
    • The synthesis of proteins upon ribosomes
    • J.D Watson The synthesis of proteins upon ribosomes Bull. Soc. Chim. Biol. 6 1964 1399 1425
    • (1964) Bull. Soc. Chim. Biol. , vol.6 , pp. 1399-1425
    • Watson, J.D1
  • 8
    • 0004124837 scopus 로고
    • Ribosome Structure and Protein Synthesis
    • A.S Spirin Ribosome Structure and Protein Synthesis 1986 The Benjamin/Cummings Publishing Company, Inc., Menlo Park, CA
    • (1986)
    • Spirin, A.S1
  • 9
    • 0025733603 scopus 로고
    • Ribosomal RNA and translation
    • H.F Noller Ribosomal RNA and translation Ann. Rev. Biochem. 60 1991 191 227
    • (1991) Ann. Rev. Biochem. , vol.60 , pp. 191-227
    • Noller, H.F1
  • 10
    • 85119558517 scopus 로고
    • Three tRNA binding sites involved in the ribosomal elongation cycle
    • K.H Nierhaus H.-J Rheinberger U Geigenmuller A Gnirke H Saruyama S Schilling P Wurmbach Three tRNA binding sites involved in the ribosomal elongation cycle B Hardesty G Kramer Structure, Function, and Genetics of Ribosomes 1986 Springer-Verlag New York 454 472
    • (1986) , pp. 454-472
    • Nierhaus, K.H1    Rheinberger, H.-J2    Geigenmuller, U3    Gnirke, A4    Saruyama, H5    Schilling, S6    Wurmbach, P7
  • 11
    • 0343438085 scopus 로고
    • The movement of tRNA through ribosomes during peptide elongation: the displacement reaction model
    • B Hardesty O.W Odom H.-Y Deng The movement of tRNA through ribosomes during peptide elongation: the displacement reaction model B Hardesty G Kramer Structure, Function, and Genetics of Ribosomes 1986 Springer-Verlag New York 495 508
    • (1986) , pp. 495-508
    • Hardesty, B1    Odom, O.W2    Deng, H.-Y3
  • 12
    • 85005635817 scopus 로고
    • Mechanism of ribosomal translocation
    • W Wintermeyer R Lill H Paulsen J.M Robertson Mechanism of ribosomal translocation B Hardesty G Kramer Structure, Function, and Genetics of Ribosomes 1986 Springer-Verlag New York 523 540
    • (1986) , pp. 523-540
    • Wintermeyer, W1    Lill, R2    Paulsen, H3    Robertson, J.M4
  • 13
    • 0025679294 scopus 로고
    • The Movement of tRNA but not nascent peptide during peptide bond formation on ribosomes
    • O.W Odom W.D Picking B Hardesty The Movement of tRNA but not nascent peptide during peptide bond formation on ribosomes Biochemistry 29 1990 10734 10744
    • (1990) Biochemistry , vol.29 , pp. 10734-10744
    • Odom, O.W1    Picking, W.D2    Hardesty, B3
  • 14
    • 0025922759 scopus 로고
    • The synthesis of polyphenylalanine on ribosomes to which erthromycin is bound
    • O.W Odom W.D Picking W Hardesty T Tsalkova The synthesis of polyphenylalanine on ribosomes to which erthromycin is bound Eur. J. Biochem. 198 1991 713 722
    • (1991) Eur. J. Biochem. , vol.198 , pp. 713-722
    • Odom, O.W1    Picking, W.D2    Hardesty, W3    Tsalkova, T4
  • 15
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • D Moazed H.F Noller Intermediate states in the movement of transfer RNA in the ribosome Nature 342 1989 142 148
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D1    Noller, H.F2
  • 16
    • 0033605751 scopus 로고    scopus 로고
    • Effect of buffer conditions on the position of tRNA on the 70S ribosome as visualized by cryoelectron microscopy
    • R.K Agrawal P Penczek R.A Grassucci N Burkhardt K.H Nierhaus J Frank Effect of buffer conditions on the position of tRNA on the 70S ribosome as visualized by cryoelectron microscopy J. Biol. Chem. 274 1999 8723 8729
    • (1999) J. Biol. Chem. , vol.274 , pp. 8723-8729
    • Agrawal, R.K1    Penczek, P2    Grassucci, R.A3    Burkhardt, N4    Nierhaus, K.H5    Frank, J6
  • 17
    • 0032502997 scopus 로고    scopus 로고
    • Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA
    • R Green C Switzer H.F Noller Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA Science 280 1998 286 289
    • (1998) Science , vol.280 , pp. 286-289
    • Green, R1    Switzer, C2    Noller, H.F3
  • 18
    • 0014219466 scopus 로고
    • Catalysis of peptide bond formation by 50S ribosomal subunits from Escherichia coli
    • R.E Monro Catalysis of peptide bond formation by 50S ribosomal subunits from Escherichia coli J. Mol. Biol. 26 1967 147 151
    • (1967) J. Mol. Biol. , vol.26 , pp. 147-151
    • Monro, R.E1
  • 19
    • 0023645140 scopus 로고
    • Destabilization of codon-anticodon interaction in the ribosomal exit site
    • R Lill W Wintermeyer Destabilization of codon-anticodon interaction in the ribosomal exit site J. Mol. Biol. 196 1987 137 148
    • (1987) J. Mol. Biol. , vol.196 , pp. 137-148
    • Lill, R1    Wintermeyer, W2
  • 20
    • 0009021316 scopus 로고
    • An apparent conformational change in tRNAPhe that is associated with the peptidyl transferase reaction
    • Phe that is associated with the peptidyl transferase reaction Biochimie 69 1987 925 938
    • (1987) Biochimie , vol.69 , pp. 925-938
    • Odom, O.W1    Hardesty, B2
  • 21
    • 0032192760 scopus 로고    scopus 로고
    • Peptidyl-transferase ribozymes: trans reactions, structural characterization and ribosomal RNA-like features
    • B Zhang T.R Cech Peptidyl-transferase ribozymes: trans reactions, structural characterization and ribosomal RNA-like features Chem. Biol. 5 1998 539 553
    • (1998) Chem. Biol. , vol.5 , pp. 539-553
    • Zhang, B1    Cech, T.R2
  • 22
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction procedures
    • H.F Noller V Hoffarth L Zimniak Unusual resistance of peptidyl transferase to protein extraction procedures Science 256 1992 1416 1419
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F1    Hoffarth, V2    Zimniak, L3
  • 23
    • 0031906988 scopus 로고    scopus 로고
    • Possible involvement of Escherichia coli 23S ribosomal RNA in peptide bond formation
    • I Nitta T Ueda K Watanabe Possible involvement of Escherichia coli 23S ribosomal RNA in peptide bond formation RNA 4 1998 257 267
    • (1998) RNA , vol.4 , pp. 257-267
    • Nitta, I1    Ueda, T2    Watanabe, K3
  • 24
    • 0032950453 scopus 로고    scopus 로고
    • Peptidyl transferase activity catalyzed by protein-free 23S ribosomal RNA remains elusive
    • P Khaitovich T Tenson A.S Mankin R Green Peptidyl transferase activity catalyzed by protein-free 23S ribosomal RNA remains elusive RNA 5 1999 605 608
    • (1999) RNA , vol.5 , pp. 605-608
    • Khaitovich, P1    Tenson, T2    Mankin, A.S3    Green, R4
  • 26
    • 0039650214 scopus 로고
    • Ribosomes and the RNA World
    • P.B Moore Ribosomes and the RNA World The RNA World 1993 Cold Spring Harbor Monograph Series Press Plainview 119 135
    • (1993) , pp. 119-135
    • Moore, P.B1
  • 27
    • 0027078664 scopus 로고
    • Evidence for RNA in the peptidyl transferase center of Escherichia coli ribosomes as indicated by fluorescence
    • W.D Picking O.W Odom B Hardesty Evidence for RNA in the peptidyl transferase center of Escherichia coli ribosomes as indicated by fluorescence Biochem. 31 1992 12565 12570
    • (1992) Biochem. , vol.31 , pp. 12565-12570
    • Picking, W.D1    Odom, O.W2    Hardesty, B3
  • 28
    • 0011206867 scopus 로고
    • Stereochemical analysis of ribosomal transpeptidation, translocation and nascent peptide folding
    • A.S Spirin V.I Lim Stereochemical analysis of ribosomal transpeptidation, translocation and nascent peptide folding B Hardesty G Kramer Structure, Function, and Genetics of Ribosomes 1986 Springer-Verlag New York 556 572
    • (1986) , pp. 556-572
    • Spirin, A.S1    Lim, V.I2
  • 29
    • 0023053308 scopus 로고
    • Stereochemical analysis of ribosomal transpeptidation. Conformation of nascent peptide
    • V.I Lim A.S Spirin Stereochemical analysis of ribosomal transpeptidation. Conformation of nascent peptide J. Mol. Biol. 188 1986 565 574
    • (1986) J. Mol. Biol. , vol.188 , pp. 565-574
    • Lim, V.I1    Spirin, A.S2
  • 30
    • 0026031835 scopus 로고
    • The conformation of nascent polylysine and polyphenylalanine peptides on ribosomes
    • W.D Picking O.W Odom T Tsalkova I Serdyuk B Hardesty The conformation of nascent polylysine and polyphenylalanine peptides on ribosomes J. Biol. Chem. 266 1991 1534 1542
    • (1991) J. Biol. Chem. , vol.266 , pp. 1534-1542
    • Picking, W.D1    Odom, O.W2    Tsalkova, T3    Serdyuk, I4    Hardesty, B5
  • 31
    • 0025140812 scopus 로고
    • The extension of polyphenylalanine and polylysine peptides on Escherichia coli ribosomes
    • B Hardesty W.D Picking O.W Odom The extension of polyphenylalanine and polylysine peptides on Escherichia coli ribosomes Biochem. Biophys. Acta 1050 1990 197 202
    • (1990) Biochem. Biophys. Acta , vol.1050 , pp. 197-202
    • Hardesty, B1    Picking, W.D2    Odom, O.W3
  • 32
    • 0025934716 scopus 로고
    • The use of synthetic tRNAs as probes for examining nascent peptides on Escherichia coli ribosomes
    • W Picking W.D Picking B Hardesty The use of synthetic tRNAs as probes for examining nascent peptides on Escherichia coli ribosomes Biochimie 73 1991 1101 1108
    • (1991) Biochimie , vol.73 , pp. 1101-1108
    • Picking, W1    Picking, W.D2    Hardesty, B3
  • 33
    • 0025993695 scopus 로고
    • A synthetic alanyl-initiator tRNA with initiator tRNA properties as determined by fluorescence measurement: comparison to a synthetic alanyl-elongator tRNA
    • W.L Picking W.D Picking C Ma B Hardesty A synthetic alanyl-initiator tRNA with initiator tRNA properties as determined by fluorescence measurement: comparison to a synthetic alanyl-elongator tRNA Nucl. Ac. Res. 19 1991 5749 5754
    • (1991) Nucl. Ac. Res. , vol.19 , pp. 5749-5754
    • Picking, W.L1    Picking, W.D2    Ma, C3    Hardesty, B4
  • 34
    • 0026591728 scopus 로고
    • Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit Escherichia coli ribosomes during translation
    • W.D Picking W.L Picking O.W Odom B Hardesty Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit Escherichia coli ribosomes during translation Biochem. 31 1992 2368 2375
    • (1992) Biochem. , vol.31 , pp. 2368-2375
    • Picking, W.D1    Picking, W.L2    Odom, O.W3    Hardesty, B4
  • 35
    • 0020134907 scopus 로고
    • Nascent polypeptide chains emerge from the exit domain of the large ribosomal subunit: immune mapping of the nascent chain
    • C Bernabeu J.A Lake Nascent polypeptide chains emerge from the exit domain of the large ribosomal subunit: immune mapping of the nascent chain 6th ed. Proc. Natl. Acad. Sci. USA 79 1982 3111 3115
    • (1982) , pp. 3111-3115
    • Bernabeu, C1    Lake, J.A2
  • 36
    • 0023212383 scopus 로고
    • A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction
    • A Yonath K.R Leonard H.G Wittmann A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction Science 236 1987 813 816
    • (1987) Science , vol.236 , pp. 813-816
    • Yonath, A1    Leonard, K.R2    Wittmann, H.G3
  • 37
    • 0344437773 scopus 로고
    • Modeling the progression of nascent proteins in ribosomes
    • M Eisenstein B Hardesty O.W Odom W Kudlicki G Kramer T Arad F Franceschi A Yonath Modeling the progression of nascent proteins in ribosomes G Pifat Supramolecular Structure and Function 1994 Balaban Publishers Rehovot, Israel 213 246
    • (1994) , pp. 213-246
    • Eisenstein, M1    Hardesty, B2    Odom, O.W3    Kudlicki, W4    Kramer, G5    Arad, T6    Franceschi, F7    Yonath, A8
  • 39
    • 0033607003 scopus 로고    scopus 로고
    • Placement of protein and RNA structures into a 5A-resolution map of the 50S ribosomal subunit
    • N Ban P Nissen J Hansen M Capel P.B Moore T.A Steitz Placement of protein and RNA structures into a 5A-resolution map of the 50S ribosomal subunit Nature 400 1999 841 847
    • (1999) Nature , vol.400 , pp. 841-847
    • Ban, N1    Nissen, P2    Hansen, J3    Capel, M4    Moore, P.B5    Steitz, T.A6
  • 40
  • 41
    • 0029055199 scopus 로고
    • Mapping the path of the nascent peptide chain through the 23S RNA in the 50S ribosomal subunit
    • K Stade N Junke R Brimacombe Mapping the path of the nascent peptide chain through the 23S RNA in the 50S ribosomal subunit Nucl. Ac. Res. 23 1995 2371 2380
    • (1995) Nucl. Ac. Res. , vol.23 , pp. 2371-2380
    • Stade, K1    Junke, N2    Brimacombe, R3
  • 42
    • 0032519376 scopus 로고    scopus 로고
    • The path of the growing peptide chain through the 23S rRNA in the 50S ribosomal subunit; a comparative cross-linking study with three different peptide families
    • K.M Choi R Brimacombe The path of the growing peptide chain through the 23S rRNA in the 50S ribosomal subunit; a comparative cross-linking study with three different peptide families Nucl. Ac. Res. 2 1998 887 895
    • (1998) Nucl. Ac. Res. , vol.2 , pp. 887-895
    • Choi, K.M1    Brimacombe, R2
  • 43
    • 0032527774 scopus 로고    scopus 로고
    • Flexibility of the nascent polypeptide chain within the ribosome. Contacts from the peptide N-terminus to a specific region of the 30S subunit
    • K.M Choi J Atkins R Gesteland R Brimacombe Flexibility of the nascent polypeptide chain within the ribosome. Contacts from the peptide N-terminus to a specific region of the 30S subunit Eur. J. Biochem. 255 1998 409 413
    • (1998) Eur. J. Biochem. , vol.255 , pp. 409-413
    • Choi, K.M1    Atkins, J2    Gesteland, R3    Brimacombe, R4
  • 44
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • W.J Netzer F.U Hard Recombination of protein domains facilitated by co-translational folding in eukaryotes Nature 388 1998 343 349
    • (1998) Nature , vol.388 , pp. 343-349
    • Netzer, W.J1    Hard, F.U2
  • 45
    • 0028849478 scopus 로고
    • Folding of an enzyme into an active conformation while bound as peptidyl-tRNA to the ribosome
    • W Kudlicki J Chirgwin G Kramer B Hardesty Folding of an enzyme into an active conformation while bound as peptidyl-tRNA to the ribosome Biochem. 34 1995 14284 14287
    • (1995) Biochem. , vol.34 , pp. 14284-14287
    • Kudlicki, W1    Chirgwin, J2    Kramer, G3    Hardesty, B4
  • 46
    • 0030025303 scopus 로고    scopus 로고
    • Enzymatic activity of the ribosome-bound nascent polypeptide
    • E.V Makeyev V.A Kolb A.S Spirin Enzymatic activity of the ribosome-bound nascent polypeptide FEBS Lett. 376 1996 166 170
    • (1996) FEBS Lett. , vol.376 , pp. 166-170
    • Makeyev, E.V1    Kolb, V.A2    Spirin, A.S3
  • 48
    • 0032525163 scopus 로고    scopus 로고
    • Different conformations of nascent peptides on ribosomes
    • T Tsalkova O.W Odom G Kramer B Hardesty Different conformations of nascent peptides on ribosomes J. Mol. Biol. 278 1998 713 723
    • (1998) J. Mol. Biol. , vol.278 , pp. 713-723
    • Tsalkova, T1    Odom, O.W2    Kramer, G3    Hardesty, B4
  • 49
    • 0026481261 scopus 로고
    • High-efficiency cell-free synthesis of proteins: refinement of the coupled transcription-translation system
    • W Kudlicki G Kramer B Hardesty High-efficiency cell-free synthesis of proteins: refinement of the coupled transcription-translation system Anal. Biochem. 206 1992 89 393
    • (1992) Anal. Biochem. , vol.206 , pp. 89-393
    • Kudlicki, W1    Kramer, G2    Hardesty, B3
  • 50
    • 0001795984 scopus 로고    scopus 로고
    • Folding of nascent peptides on ribosomes
    • B Hardesty G Kramer T Tsalkova V Ramachandiran B McIntosh D Brod Folding of nascent peptides on ribosomes R Garrett A Douthwaite A Liljas A Matheson P Moore H Noller The Ribosome: Structure, Function, Antibiotics and Cellular Interactions 2000 ASM Press Washington, D.C 287 297
    • (2000) , pp. 287-297
    • Hardesty, B1    Kramer, G2    Tsalkova, T3    Ramachandiran, V4    McIntosh, B5    Brod, D6
  • 51
    • 0033548227 scopus 로고    scopus 로고
    • The effect of a hydrophobic N-terminal probe on translational pausing of chloramphenicol acetyl transferase and rhodanese
    • T Tsalkova G Kramer B Hardesty The effect of a hydrophobic N-terminal probe on translational pausing of chloramphenicol acetyl transferase and rhodanese J. Mol. Biol. 286 1999 71 81
    • (1999) J. Mol. Biol. , vol.286 , pp. 71-81
    • Tsalkova, T1    Kramer, G2    Hardesty, B3
  • 52
    • 0032967390 scopus 로고    scopus 로고
    • N-terminal and C-terminal modifications affect folding, release from the ribosomes and stability of in vitro synthesized proteins
    • G Kramer W Kudlicki D McCarthy T Tsalkova D Simmons B Hardesty N-terminal and C-terminal modifications affect folding, release from the ribosomes and stability of in vitro synthesized proteins Int. J. Biochem. and Cell Biol. 31 1999 231 241
    • (1999) Int. J. Biochem. and Cell Biol. , vol.31 , pp. 231-241
    • Kramer, G1    Kudlicki, W2    McCarthy, D3    Tsalkova, T4    Simmons, D5    Hardesty, B6
  • 53
    • 0030048409 scopus 로고    scopus 로고
    • In vitro protein folding by ribosomes from Escherichia coli, wheat germ and rat liver
    • B Das S Chattopadhyay A.K Bera C Dasgupta In vitro protein folding by ribosomes from Escherichia coli , wheat germ and rat liver Eur. J. Biochem. 235 1996 613 621
    • (1996) Eur. J. Biochem. , vol.235 , pp. 613-621
    • Das, B1    Chattopadhyay, S2    Bera, A.K3    Dasgupta, C4
  • 54
    • 0030623528 scopus 로고    scopus 로고
    • Ribosomes and ribosomal RNA as chaperones for folding of proteins
    • W Kudlicki A Coffman G Kramer B Hardesty Ribosomes and ribosomal RNA as chaperones for folding of proteins Folding & Design 2 1997 101 108
    • (1997) Folding & Design , vol.2 , pp. 101-108
    • Kudlicki, W1    Coffman, A2    Kramer, G3    Hardesty, B4
  • 55
    • 0020479406 scopus 로고
    • The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28S ribosomal ribonucleic acid
    • Y Endo I.G Wool The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28S ribosomal ribonucleic acid J. Biol. Chem. 257 1982 9054
    • (1982) J. Biol. Chem. , vol.257 , pp. 9054
    • Endo, Y1    Wool, I.G2
  • 56
    • 0026764794 scopus 로고
    • The two main states of the elongating ribosome and the role of the alpha-sarcin stem-loop structure of 23S RNA
    • K.H Nierhaus S Schilling-Bartetzko T Twardowski The two main states of the elongating ribosome and the role of the alpha-sarcin stem-loop structure of 23S RNA Biochimie 74 1992 403 410
    • (1992) Biochimie , vol.74 , pp. 403-410
    • Nierhaus, K.H1    Schilling-Bartetzko, S2    Twardowski, T3
  • 57
    • 0028227364 scopus 로고
    • Structural dynamics of translating ribosomes: 16S ribosomal RNA bases that may move twice during translocation
    • M Laughrea Structural dynamics of translating ribosomes: 16S ribosomal RNA bases that may move twice during translocation Mol. Microbiol. 11 1994 999 1007
    • (1994) Mol. Microbiol. , vol.11 , pp. 999-1007
    • Laughrea, M1
  • 58
    • 0028135617 scopus 로고
    • Synergism between the GTPase activities of EF-Tu.GTP and EF-G.GTP on empty ribosomes. Elongation factors as stimulators of the ribosomal oscillation between two conformations
    • J.R Mesters A.P Potapov J.M de Graaf B Kraal Synergism between the GTPase activities of EF-Tu.GTP and EF-G.GTP on empty ribosomes. Elongation factors as stimulators of the ribosomal oscillation between two conformations J. Mol. Biol. 242 1994 644 654
    • (1994) J. Mol. Biol. , vol.242 , pp. 644-654
    • Mesters, J.R1    Potapov, A.P2    de Graaf, J.M3    Kraal, B4
  • 59
    • 0033602228 scopus 로고    scopus 로고
    • Molecular chaperones: Pathways and networks
    • J Ellis Molecular chaperones: Pathways and networks Current Biology 9 1999 R137 R139
    • (1999) Current Biology , vol.9 , pp. R137-R139
    • Ellis, J1
  • 60
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of chaperonin proteins in protein folding in vivo
    • G.H Lorimer A quantitative assessment of the role of chaperonin proteins in protein folding in vivo FASEB J. 10 1996 5 9
    • (1996) FASEB J. , vol.10 , pp. 5-9
    • Lorimer, G.H1
  • 61
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • K.L Ewalt J.P Hendrick W.A Houry F.U Hard In vivo observation of polypeptide flux through the bacterial chaperonin system Cell 90 1997 491 500
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L1    Hendrick, J.P2    Houry, W.A3    Hard, F.U4
  • 62
    • 0027322659 scopus 로고
    • GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation
    • T Tsalkova G Zardeneta W Kudlicki G Kramer P.M Horowitz B Hardesty GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation Biochemistry 32 1993 3377 3380
    • (1993) Biochemistry , vol.32 , pp. 3377-3380
    • Tsalkova, T1    Zardeneta, G2    Kudlicki, W3    Kramer, G4    Horowitz, P.M5    Hardesty, B6
  • 63
    • 0028346454 scopus 로고
    • Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNA
    • W Kudlicki O.W Odom G Kramer B Hardesty Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNA J. Biol. Chem. 269 1994 16549 16553
    • (1994) J. Biol. Chem. , vol.269 , pp. 16549-16553
    • Kudlicki, W1    Odom, O.W2    Kramer, G3    Hardesty, B4
  • 64
    • 0027988581 scopus 로고
    • Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese: analysis by fluorescence
    • W Kudlicki O.W Odom G Kramer B Hardesty Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese: analysis by fluorescence J. Mol. Biol. 244 1994 319 331
    • (1994) J. Mol. Biol. , vol.244 , pp. 319-331
    • Kudlicki, W1    Odom, O.W2    Kramer, G3    Hardesty, B4
  • 65
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • F.U Hard Molecular chaperones in cellular protein folding Nature 381 1996 571 580
    • (1996) Nature , vol.381 , pp. 571-580
    • Hard, F.U1
  • 66
    • 0026649409 scopus 로고
    • The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
    • R.J Nelson T Ziegelhoffer C Nicolet M Werner-Washburne E.A Craig The translation machinery and 70 kd heat shock protein cooperate in protein synthesis Cell 71 1992 97 105
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J1    Ziegelhoffer, T2    Nicolet, C3    Werner-Washburne, M4    Craig, E.A5
  • 67
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • D.K Eggers W.J Welch W Hansen Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells Mol. Biol. Cell 8 1997 1559 1573
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1559-1573
    • Eggers, D.K1    Welch, W.J2    Hansen, W3
  • 68
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • V Thulasiraman C.-F Yang J Frydman In vivo newly translated polypeptides are sequestered in a protected folding environment EMBO J. 18 1999 85 95
    • (1999) EMBO J. , vol.18 , pp. 85-95
    • Thulasiraman, V1    Yang, C.-F2    Frydman, J3
  • 69
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • A.L Fink Chaperone-mediated protein folding Physiol. Rev. 79 1999 425 429
    • (1999) Physiol. Rev. , vol.79 , pp. 425-429
    • Fink, A.L1
  • 70
    • 0033616741 scopus 로고    scopus 로고
    • Dnaj dramatically stimulates ATP hydrolysis by DnaK: insight into targeting of Hsp70 proteins to polypeptide substrates
    • R Russell W Karzai A.F Mehl R McMacken Dnaj dramatically stimulates ATP hydrolysis by DnaK: insight into targeting of Hsp70 proteins to polypeptide substrates Biochem. 38 1999 4165 4176
    • (1999) Biochem. , vol.38 , pp. 4165-4176
    • Russell, R1    Karzai, W2    Mehl, A.F3    McMacken, R4
  • 71
    • 0041734594 scopus 로고    scopus 로고
    • Structural features required for the interaction of the hsp70 molecular chaperone DnaK with its cochaperone DnaJ
    • W.C Suh C.Z Lu C.A Gross Structural features required for the interaction of the hsp70 molecular chaperone DnaK with its cochaperone DnaJ J. Biol. Chem. 274 1999 30534 30539
    • (1999) J. Biol. Chem. , vol.274 , pp. 30534-30539
    • Suh, W.C1    Lu, C.Z2    Gross, C.A3
  • 73
    • 0030945296 scopus 로고    scopus 로고
    • GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism
    • L Packschies H Theyssen A Buchberger B Bukau R.S Goody J Reinstein GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism Biochem. 36 1997 3417 3422
    • (1997) Biochem. , vol.36 , pp. 3417-3422
    • Packschies, L1    Theyssen, H2    Buchberger, A3    Bukau, B4    Goody, R.S5    Reinstein, J6
  • 74
    • 0032549525 scopus 로고    scopus 로고
    • Control of the DnaK chaperone cycle by substoichiometric concentrations of the co-chaperones DnaJ and GrPE
    • E.V Pierpaoli E Sandmeier H.J Schonfeld P Christen Control of the DnaK chaperone cycle by substoichiometric concentrations of the co-chaperones DnaJ and GrPE J. Biol. Chem. 273 1998 6643 6649
    • (1998) J. Biol. Chem. , vol.273 , pp. 6643-6649
    • Pierpaoli, E.V1    Sandmeier, E2    Schonfeld, H.J3    Christen, P4
  • 75
    • 0028929052 scopus 로고
    • The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components
    • H.J Schonfeld D Schmidt H Schroder B Bukau The DnaK chaperone system of Escherichia coli : quaternary structures and interactions of the DnaK and GrpE components J. Biol. Chem. 270 1995 2183 2189
    • (1995) J. Biol. Chem. , vol.270 , pp. 2183-2189
    • Schonfeld, H.J1    Schmidt, D2    Schroder, H3    Bukau, B4
  • 76
    • 0028943041 scopus 로고
    • The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNA
    • W Kudlicki O.W Odom G Kramer B Hardesty G.A Merrill P.M Horowitz The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNA J. Biol. Chem. 270 1995 10650 10657
    • (1995) J. Biol. Chem. , vol.270 , pp. 10650-10657
    • Kudlicki, W1    Odom, O.W2    Kramer, G3    Hardesty, B4    Merrill, G.A5    Horowitz, P.M6
  • 77
    • 0029563006 scopus 로고
    • Inhibition of the release factor-dependent termination reaction on ribosomes by DnaJ and the N-terminal peptide of rhodanese
    • W Kudlicki O.W Ddom G Merrill G Kramer B Hardesty Inhibition of the release factor-dependent termination reaction on ribosomes by DnaJ and the N-terminal peptide of rhodanese J. Bacteriol. 177 1995 5517 5522
    • (1995) J. Bacteriol. , vol.177 , pp. 5517-5522
    • Kudlicki, W1    Ddom, O.W2    Merrill, G3    Kramer, G4    Hardesty, B5
  • 78
    • 0032561078 scopus 로고    scopus 로고
    • Truncations at the NH2 terminus of rhodanese destabilize the enzyme and decrease its heterologous expression
    • R.J Trevino T Tsalkova G Kramer B Hardesty J.M Chirgwin P Horowitz Truncations at the NH2 terminus of rhodanese destabilize the enzyme and decrease its heterologous expression J. Biol. Chem. 273 1998 27841 27847
    • (1998) J. Biol. Chem. , vol.273 , pp. 27841-27847
    • Trevino, R.J1    Tsalkova, T2    Kramer, G3    Hardesty, B4    Chirgwin, J.M5    Horowitz, P6
  • 79
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • G Stoller K.P Rücknagel K Nierhaus F.X Schmid G Fischer J.U Rahfeld A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor EMBO J. 14 1995 4939 4948
    • (1995) EMBO J. , vol.14 , pp. 4939-4948
    • Stoller, G1    Rücknagel, K.P2    Nierhaus, K3    Schmid, F.X4    Fischer, G5    Rahfeld, J.U6
  • 80
    • 0031554922 scopus 로고    scopus 로고
    • Modular structure of the trigger factor required for high activity in protein folding
    • T Zarnt T Tradler G Stoller C Scholz F.X Schmid G Fischer Modular structure of the trigger factor required for high activity in protein folding J. Mol. Biol. 271 1997 827 837
    • (1997) J. Mol. Biol. , vol.271 , pp. 827-837
    • Zarnt, T1    Tradler, T2    Stoller, G3    Scholz, C4    Schmid, F.X5    Fischer, G6
  • 81
    • 0030881913 scopus 로고    scopus 로고
    • The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
    • T Hesterkamp E Deuerling B Bukau The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes J. Biol. Chem. 272 1997 21865 21871
    • (1997) J. Biol. Chem. , vol.272 , pp. 21865-21871
    • Hesterkamp, T1    Deuerling, E2    Bukau, B3
  • 82
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides
    • Q.A Valent D.A Kendall S High R Kusters B Oudega J Luirink Early events in preprotein recognition in E. coli : interaction of SRP and trigger factor with nascent polypeptides EMBO J. 14 1995 5494
    • (1995) EMBO J. , vol.14 , pp. 5494
    • Valent, Q.A1    Kendall, D.A2    High, S3    Kusters, R4    Oudega, B5    Luirink, J6
  • 83
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains
    • T Hesterkamp S Hauser H Lütcke B Bukau Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains 6th ed. Proc. Natl. Acad. Sci. USA 93 1996 4437 4441
    • (1996) , pp. 4437-4441
    • Hesterkamp, T1    Hauser, S2    Lütcke, H3    Bukau, B4
  • 84
    • 0033032592 scopus 로고    scopus 로고
    • Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
    • S.A Teter W.A Houry D Ang T Tradler D Rockabrand G Fischer P Blum C Georgopoulos F.U Hard Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains Cell 97 1999 755 765
    • (1999) Cell , vol.97 , pp. 755-765
    • Teter, S.A1    Houry, W.A2    Ang, D3    Tradler, T4    Rockabrand, D5    Fischer, G6    Blum, P7    Georgopoulos, C8    Hard, F.U9
  • 85
    • 0033549770 scopus 로고    scopus 로고
    • Trigger factor and DnaK cooperate in folding of newly synthesized proteins
    • E Deuerling A Schulze-Specking T Tomoyasu A Mogk B Bukau Trigger factor and DnaK cooperate in folding of newly synthesized proteins Nature 400 1999 693 696
    • (1999) Nature , vol.400 , pp. 693-696
    • Deuerling, E1    Schulze-Specking, A2    Tomoyasu, T3    Mogk, A4    Bukau, B5


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