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Volumn 74, Issue 8, 1996, Pages 423-439

Throwing a spanner in the works: Antibiotics and the translation apparatus

Author keywords

Antibiotics; Elongation factors; Ribosomal RNA; Ribosomes

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; CHLORAMPHENICOL; ELONGATION FACTOR; ERYTHROMYCIN; FUSIDIC ACID; GENTAMICIN; INITIATION FACTOR; KANAMYCIN; LINCOMYCIN; MACROLIDE; MIKAMYCIN B; MOCIMYCIN; NEOMYCIN; PEPTIDYLTRANSFERASE; POLYPEPTIDE ANTIBIOTIC AGENT; PUROMYCIN; RIBOSOME RNA; RNA 16S; SPECTINOMYCIN; SPIRAMYCIN; TETRACYCLINE; THIOSTREPTON; VIOMYCIN; VIRGINIAMYCIN;

EID: 0029745623     PISSN: 09462716     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00217518     Document Type: Review
Times cited : (176)

References (150)
  • 1
    • 0003693926 scopus 로고
    • Biochemie der Antibiotika: Struktur-Biosynthese-Wirkmechanismus
    • Heidelberg Berlin New York
    • Gräfe U (1992) Biochemie der Antibiotika: Struktur-Biosynthese-Wirkmechanismus. Spektrum, Heidelberg Berlin New York
    • (1992) Spektrum
    • Gräfe, U.1
  • 3
    • 9344266445 scopus 로고
    • Inhibition of protein biosynthesis by antibiotics
    • Jackson GG, Schlumberger HD, Zeiler HJ (eds) Vieweg, Braunschweig Wiesbaden
    • Nierhaus KH, Brimacombe R, Witiniann HG (1988) Inhibition of protein biosynthesis by antibiotics. In: Jackson GG, Schlumberger HD, Zeiler HJ (eds) Perspectives in antiinfective therapy. Vieweg, Braunschweig Wiesbaden
    • (1988) Perspectives in Antiinfective Therapy
    • Nierhaus, K.H.1    Brimacombe, R.2    Witiniann, H.G.3
  • 4
    • 0040980982 scopus 로고
    • Structure of ribosomes
    • Hardesty B, Kramer G (eds) Springer, Berlin Heidelberg New York
    • Wittmann HG (1986) Structure of ribosomes. In: Hardesty B, Kramer G (eds) Structure, function, and genetics of ribosomes. Springer, Berlin Heidelberg New York, pp 1-27
    • (1986) Structure, Function, and Genetics of Ribosomes , pp. 1-27
    • Wittmann, H.G.1
  • 5
    • 0025733603 scopus 로고
    • Ribosomal RNA and translation
    • Noller HF (1991) Ribosomal RNA and translation. Annu Rev Biochem 60:191-227
    • (1991) Annu Rev Biochem , vol.60 , pp. 191-227
    • Noller, H.F.1
  • 6
    • 0003074704 scopus 로고
    • Sequence comparison and evolution of ribosomal proteins and their genes
    • Hill WE, Dahlberg A, Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) American Society for Microbiology, Washington
    • Wittmann-Liebold B, Köpke AKE, Arndt E, Krömer W, Hatakeyama T, Wittmann HG (1990) Sequence comparison and evolution of ribosomal proteins and their genes. In: Hill WE, Dahlberg A, Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) The ribosome. Structure function and evolution. American Society for Microbiology, Washington, pp 598-616
    • (1990) The Ribosome. Structure Function and Evolution , pp. 598-616
    • Wittmann-Liebold, B.1    Köpke, A.K.E.2    Arndt, E.3    Krömer, W.4    Hatakeyama, T.5    Wittmann, H.G.6
  • 7
    • 0028071557 scopus 로고
    • Collection of small subunit (16S- and 16S-like) ribosomal RNA structures: 1994
    • Gutell RR (1994) Collection of small subunit (16S- and 16S-like) ribosomal RNA structures: 1994. Nucleic Acids Res 22:3502-3507
    • (1994) Nucleic Acids Res , vol.22 , pp. 3502-3507
    • Gutell, R.R.1
  • 8
    • 0027225783 scopus 로고
    • A compilation of large subunit (23S- and 23S-like) ribosomal RNA structures
    • Gutell RR, Gray MW, Schnare MN (1993) A compilation of large subunit (23S- and 23S-like) ribosomal RNA structures. Nucleic Acids Res 21:3055-3074
    • (1993) Nucleic Acids Res , vol.21 , pp. 3055-3074
    • Gutell, R.R.1    Gray, M.W.2    Schnare, M.N.3
  • 9
    • 0024278056 scopus 로고
    • A detailed model for the three-dimensional structure of E. coli 16S ribosomal RNA in situ in the 30S subunit
    • Brimacombe R, Amadja J, Stiege W, Schüler D (1988) A detailed model for the three-dimensional structure of E. coli 16S ribosomal RNA in situ in the 30S subunit. J Mol Biol 199:115-136
    • (1988) J Mol Biol , vol.199 , pp. 115-136
    • Brimacombe, R.1    Amadja, J.2    Stiege, W.3    Schüler, D.4
  • 10
    • 0024293439 scopus 로고
    • Model for the three-dimensional folding of 16S ribosomal RNA
    • Stern S, Weiser B, Noller HF (1988) Model for the three-dimensional folding of 16S ribosomal RNA. J Mol Biol 204: 447-481
    • (1988) J Mol Biol , vol.204 , pp. 447-481
    • Stern, S.1    Weiser, B.2    Noller, H.F.3
  • 11
    • 0029044829 scopus 로고
    • The structure of ribosomal RNA: A three-dimensional jigsaw puzzle
    • Brimacombe R (1995) The structure of ribosomal RNA: a three-dimensional jigsaw puzzle. Eur J Biochem 230:365-383
    • (1995) Eur J Biochem , vol.230 , pp. 365-383
    • Brimacombe, R.1
  • 12
    • 0025140986 scopus 로고
    • Selective isolation and detailed analysis of intra-RNA crosslinks induced in the large ribosomal subunit of Escherichia coli: A model for the tertiary structure of the tRNA binding domain in 23S RNA
    • Mitchell P, Osswald M, Schüler D, Brimacombe R (1990) Selective isolation and detailed analysis of intra-RNA crosslinks induced in the large ribosomal subunit of Escherichia coli: a model for the tertiary structure of the tRNA binding domain in 23S RNA. Nucleic Acids Res 18:4325-4333
    • (1990) Nucleic Acids Res , vol.18 , pp. 4325-4333
    • Mitchell, P.1    Osswald, M.2    Schüler, D.3    Brimacombe, R.4
  • 16
    • 0028099604 scopus 로고
    • Solution scattering from 50S ribosomal subunit resolves inconsistency between electron microscopic models
    • Svergun DI, Pedersen JS, Serdyuk IN, Koch MH (1994) Solution scattering from 50S ribosomal subunit resolves inconsistency between electron microscopic models. Proc Natl Acad Sci USA 91:11826-11830
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11826-11830
    • Svergun, D.I.1    Pedersen, J.S.2    Serdyuk, I.N.3    Koch, M.H.4
  • 18
    • 0026533909 scopus 로고
    • Inter-protein distances within the large subunit from Escherichia coli ribosomes
    • May RP, Nowotny V, Nowotny P, Voss H, Nierhaus KH (1991) Inter-protein distances within the large subunit from Escherichia coli ribosomes. EMBO J 11:373-378
    • (1991) EMBO J , vol.11 , pp. 373-378
    • May, R.P.1    Nowotny, V.2    Nowotny, P.3    Voss, H.4    Nierhaus, K.H.5
  • 19
    • 0024121250 scopus 로고
    • A model for the spatial arrangement of the proteins in the large subunit of Escherichia coli ribosome
    • Walleczek J, Schüler D, Stöffler-Meilicke M, Brimacombe R, Sẗoffler G (1988) A model for the spatial arrangement of the proteins in the large subunit of Escherichia coli ribosome. EMBO J 7:3571-3576
    • (1988) EMBO J , vol.7 , pp. 3571-3576
    • Walleczek, J.1    Schüler, D.2    Stöffler-Meilicke, M.3    Brimacombe, R.4    Sẗoffler, G.5
  • 20
    • 0026773205 scopus 로고
    • Approaching atomic resolution in crystallography of ribosomes
    • Yonath A (1992) Approaching atomic resolution in crystallography of ribosomes. Ann Rev Biophys Biomol Struc 21:77-93
    • (1992) Ann Rev Biophys Biomol Struc , vol.21 , pp. 77-93
    • Yonath, A.1
  • 21
    • 0005265313 scopus 로고
    • Initiation of protein biosynthesis in procaryotes: Recognition of mRNA by ribosomes and molecular basis for the function of initiation factors
    • Hill WE, Dahlberg A, Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) American Society for Microbiology, Washington
    • Gualerzi CO, La Teana A, Spurio R, Canonaco MA, Severini M. Pon CL (1990) Initiation of protein biosynthesis in procaryotes: recognition of mRNA by ribosomes and molecular basis for the function of initiation factors. In: Hill WE, Dahlberg A, Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) The ribosome. Structure function and evolution. American Society for Microbiology, Washington, pp 281-291
    • (1990) The Ribosome. Structure Function and Evolution , pp. 281-291
    • Gualerzi, C.O.1    La Teana, A.2    Spurio, R.3    Canonaco, M.A.4    Severini, M.5    Pon, C.L.6
  • 22
    • 0026608933 scopus 로고
    • Translational termination: "stop" for protein synthesis or "pause" for regulation of gene expression
    • Tate WP, Brown CM (1992) Translational termination: "stop" for protein synthesis or "pause" for regulation of gene expression. Biochemistry 31:2443-2450
    • (1992) Biochemistry , vol.31 , pp. 2443-2450
    • Tate, W.P.1    Brown, C.M.2
  • 24
    • 0027272286 scopus 로고
    • Solution of the ribosomal riddle: How the ribosome selects the correct aminoacyl-tRNA out of 41 similar contestants
    • Nierhaus KH (1993) Solution of the ribosomal riddle: how the ribosome selects the correct aminoacyl-tRNA out of 41 similar contestants. Mol Microbiol 9:661-669
    • (1993) Mol Microbiol , vol.9 , pp. 661-669
    • Nierhaus, K.H.1
  • 25
    • 0022916242 scopus 로고
    • Transfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes
    • Moazed D, Noller HF (1986) Transfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes. Cell 47:985-994
    • (1986) Cell , vol.47 , pp. 985-994
    • Moazed, D.1    Noller, H.F.2
  • 26
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23S rRNA in the ribosomal A, P and E sites
    • Moazed D, Noller HF (1989) Interaction of tRNA with 23S rRNA in the ribosomal A, P and E sites. Cell 57:585-597
    • (1989) Cell , vol.57 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 27
    • 0024458904 scopus 로고
    • Intermediate states in the movement of tRNA in the ribosome
    • Moazed D, Noller HF (1989) Intermediate states in the movement of tRNA in the ribosome. Nature 342:142-148
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 28
    • 0029096083 scopus 로고
    • Interaction of tRNAs with the ribosome at the A and P sites
    • Dabrowski M, Spahn CMT, Nierhaus KH (1995) Interaction of tRNAs with the ribosome at the A and P sites. EMBO J: 14:4872-4882
    • (1995) EMBO J , vol.14 , pp. 4872-4882
    • Dabrowski, M.1    Spahn, C.M.T.2    Nierhaus, K.H.3
  • 30
    • 0343438085 scopus 로고
    • The movement of tRNA through ribosomes during peptide elongation: The displacement reaction model
    • Hardesly B. Kramer G (eds) Springer, Berlin Heidelberg New York
    • Hardesty B, Odom OW, Deng H-Y (1986) The movement of tRNA through ribosomes during peptide elongation: the displacement reaction model. In: Hardesly B. Kramer G (eds) Structure, function and, genetics of ribosomes. Springer, Berlin Heidelberg New York, pp 495-508
    • (1986) Structure, Function and, Genetics of Ribosomes , pp. 495-508
    • Hardesty, B.1    Odom, O.W.2    Deng, H.-Y.3
  • 31
    • 0030574576 scopus 로고    scopus 로고
    • An elongation factor turn-on
    • Nierhaus KH (1996) An elongation factor turn-on. Nature 379:491-492
    • (1996) Nature , vol.379 , pp. 491-492
    • Nierhaus, K.H.1
  • 32
    • 0023741257 scopus 로고
    • The allosteric three-site model for the elongation cycle: New insight into the inhibition mechanisms of aminoglycosides, thiostrepton, and viomycin
    • Hausner TP, Geigenmüller U, Nierhaus KH (1988) The allosteric three-site model for the elongation cycle: new insight into the inhibition mechanisms of aminoglycosides, thiostrepton, and viomycin. J Biol Chem 263:13103-13111
    • (1988) J Biol Chem , vol.263 , pp. 13103-13111
    • Hausner, T.P.1    Geigenmüller, U.2    Nierhaus, K.H.3
  • 33
    • 0026783192 scopus 로고
    • Kinetic and thermodynamic parameters for tRNA binding to the ribosome and for the translocation reaction
    • Schilling-Bartelzko S, Bartetzko A, Nierhaus KH (1992) Kinetic and thermodynamic parameters for tRNA binding to the ribosome and for the translocation reaction. J Biol Chem 267:4703-4712
    • (1992) J Biol Chem , vol.267 , pp. 4703-4712
    • Schilling-Bartelzko, S.1    Bartetzko, A.2    Nierhaus, K.H.3
  • 34
    • 0028135617 scopus 로고
    • Synergism between the GTPase activities of EF-Tu-GTP and EFG-GTP on empty ribosomes. Elongation factors as stimulators of the ribosomal oscillation between two conformations
    • Mesters JR, Polapov AP, de Graaf JM, Kraal B (1994) Synergism between the GTPase activities of EF-Tu-GTP and EFG-GTP on empty ribosomes. Elongation factors as stimulators of the ribosomal oscillation between two conformations. J Mol Biol 242:644-654
    • (1994) J Mol Biol , vol.242 , pp. 644-654
    • Mesters, J.R.1    Polapov, A.P.2    De Graaf, J.M.3    Kraal, B.4
  • 35
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski J, Wang J, Steitz TA, Moore PB (1994) The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J 13:3661-3668
    • (1994) EMBO J , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 38
    • 0025678448 scopus 로고
    • Significance of the third tRNA binding site, the E site, on E. coli ribosomes tor the accuracy of translation: An occupied E site prevents the binding of non-connate aminoacyl-tRNA to the A site
    • Geigenmüller U, Nierhaus KH (1990) Significance of the third tRNA binding site, the E site, on E. coli ribosomes tor the accuracy of translation: an occupied E site prevents the binding of non-connate aminoacyl-tRNA to the A site. EMBO J 9:4527-4533
    • (1990) EMBO J , vol.9 , pp. 4527-4533
    • Geigenmüller, U.1    Nierhaus, K.H.2
  • 39
    • 0028043424 scopus 로고
    • Translation, dissecting RNA function
    • Schroeder R (1994) Translation, dissecting RNA function. Nature .370:597-598
    • (1994) Nature , vol.370 , pp. 597-598
    • Schroeder, R.1
  • 40
    • 0002331708 scopus 로고
    • Recognition Sites for Antibiotics in rRNA
    • Hill WE, Dahlberg A, Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) American Society for Microbiology, Washington
    • Cundliffe E (1990) Recognition Sites for Antibiotics in rRNA. In: Hill WE, Dahlberg A, Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) The Ribosome. Structure Function and Evolution, American Society for Microbiology, Washington, pp 479-490
    • (1990) The Ribosome. Structure Function and Evolution , pp. 479-490
    • Cundliffe, E.1
  • 41
    • 0026690643 scopus 로고
    • Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation
    • Wool IG, Glück A, Endo Y (1992) Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation. Trends Biochem Sci 17:266-269
    • (1992) Trends Biochem Sci , vol.17 , pp. 266-269
    • Wool, I.G.1    Glück, A.2    Endo, Y.3
  • 42
    • 0028138280 scopus 로고
    • Interaction of a small RNA with antibiotic and RNA ligands of the 30S subunit
    • Purohit P, Stern S (1994) Interaction of a small RNA with antibiotic and RNA ligands of the 30S subunit. Nature 370:659-662
    • (1994) Nature , vol.370 , pp. 659-662
    • Purohit, P.1    Stern, S.2
  • 43
    • 0029051827 scopus 로고
    • Ribosomal decoding processes at codons in the A or P sites depend differently on 2′OH groups
    • Potapov AP, Triana-Alonso FJ, Nierhaus KH (1995) Ribosomal decoding processes at codons in the A or P sites depend differently on 2′OH groups. J Mol Biol 270:17680-17684
    • (1995) J Mol Biol , vol.270 , pp. 17680-17684
    • Potapov, A.P.1    Triana-Alonso, F.J.2    Nierhaus, K.H.3
  • 46
    • 0029087624 scopus 로고
    • Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies
    • Urlaub H, Kruft V, Bischof O, Müller E-C, Wittmann-Liebold B (1995) Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J 14:4578-4588
    • (1995) EMBO J , vol.14 , pp. 4578-4588
    • Urlaub, H.1    Kruft, V.2    Bischof, O.3    Müller, E.-C.4    Wittmann-Liebold, B.5
  • 47
    • 0028233867 scopus 로고
    • Analysis of the puromycin binding site in the 70 S ribosome of Escherichia coli at the peptide level
    • Bischof O, Kruft V, Wittmann-Liebold B (1994) Analysis of the puromycin binding site in the 70 S ribosome of Escherichia coli at the peptide level. J Biol Chem 269:18315-18319
    • (1994) J Biol Chem , vol.269 , pp. 18315-18319
    • Bischof, O.1    Kruft, V.2    Wittmann-Liebold, B.3
  • 48
    • 0029122856 scopus 로고
    • Peptide environment of the peptidyl transferase center from Escherichia coli 70 S ribosomes as determined by thermoaffinity labeling with dihydrospiramycin
    • Bischof O, Urlaub H, Kruft V, Wittmann-Liebold B (1995) Peptide environment of the peptidyl transferase center from Escherichia coli 70 S ribosomes as determined by thermoaffinity labeling with dihydrospiramycin. J Biol Chem 270:23060-23064
    • (1995) J Biol Chem , vol.270 , pp. 23060-23064
    • Bischof, O.1    Urlaub, H.2    Kruft, V.3    Wittmann-Liebold, B.4
  • 49
    • 0022881139 scopus 로고
    • Tetracycline can inhibit tRNA binding to the ribosomal P site as well as to the A site
    • Geigenmüller U, Nierhaus KH (1986) Tetracycline can inhibit tRNA binding to the ribosomal P site as well as to the A site. Eur J Biochem 161:723-726
    • (1986) Eur J Biochem , vol.161 , pp. 723-726
    • Geigenmüller, U.1    Nierhaus, K.H.2
  • 50
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed D, Noller HF (1987) Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature 327:389-394
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 51
    • 0001651532 scopus 로고
    • Through the accuracy window
    • Hill WE, Dahlberg A, Garrett RA, Moore PM, Sehlessinger D, Warner JR (eds) American Society for Microbiology, Washington
    • Kurland CG, Jörgensen F, Richter A, Ehrenberg M, Bilgin N, Rojas AM (1990) Through the accuracy window. In: Hill WE, Dahlberg A, Garrett RA, Moore PM, Sehlessinger D, Warner JR (eds) The ribosome. Structure function and evolution. American Society for Microbiology, Washington, pp 513-526
    • (1990) The Ribosome. Structure Function and Evolution , pp. 513-526
    • Kurland, C.G.1    Jörgensen, F.2    Richter, A.3    Ehrenberg, M.4    Bilgin, N.5    Rojas, A.M.6
  • 53
    • 0015821578 scopus 로고
    • Proteins involved in the binding of dihydrostreptomycin to ribosomes of Escherichia coli
    • Schreiner G, Nierhaus KH (1973) Proteins involved in the binding of dihydrostreptomycin to ribosomes of Escherichia coli. J Mol Biol 81:71-82
    • (1973) J Mol Biol , vol.81 , pp. 71-82
    • Schreiner, G.1    Nierhaus, K.H.2
  • 54
    • 0028348364 scopus 로고
    • Location of the streptomycin ribosomal binding site explains its pleiotropic effects on protein biosynthesis
    • Abad JP, Amilis R (1994) Location of the streptomycin ribosomal binding site explains its pleiotropic effects on protein biosynthesis. J Mol Biol 235:1251-1260
    • (1994) J Mol Biol , vol.235 , pp. 1251-1260
    • Abad, J.P.1    Amilis, R.2
  • 55
    • 0023054135 scopus 로고
    • E. coli ribosomes with a C912 to U base change in the 16S rRNA are steptomycin resistant
    • Montadon PE, Wagner R, Stutz E (1986) E. coli ribosomes with a C912 to U base change in the 16S rRNA are steptomycin resistant. EMBO J 5:3705-3708
    • (1986) EMBO J , vol.5 , pp. 3705-3708
    • Montadon, P.E.1    Wagner, R.2    Stutz, E.3
  • 56
    • 0025916683 scopus 로고
    • Mutations in the 915 region of Escherichia coli 16S ribosomal RNA reduce the binding of streptomycin to the ribosome
    • Leclerc L, Melançon P, Brakier-Gingras L (1991) Mutations in the 915 region of Escherichia coli 16S ribosomal RNA reduce the binding of streptomycin to the ribosome. Nucleic Acids Res 19:3973-3977
    • (1991) Nucleic Acids Res , vol.19 , pp. 3973-3977
    • Leclerc, L.1    Melançon, P.2    Brakier-Gingras, L.3
  • 57
    • 0023226742 scopus 로고
    • Cross-linking of streptomycin to the 16S ribosomal RNA of Escherichia coli
    • Leclerc D, Melancon P, Brakier-Gingras L (1987) Cross-linking of streptomycin to the 16S ribosomal RNA of Escherichia coli. Biochemistry 26:6227-6232
    • (1987) Biochemistry , vol.26 , pp. 6227-6232
    • Leclerc, D.1    Melancon, P.2    Brakier-Gingras, L.3
  • 58
    • 0028853679 scopus 로고
    • Genetic and comparative analyses reveal an alternative secondary structure in the region of nt 912 of Escherichia coli 16S rRNA
    • Lodmell JS, Gutell RR, Dahlberg AE (1995) Genetic and comparative analyses reveal an alternative secondary structure in the region of nt 912 of Escherichia coli 16S rRNA. Proc Natl Acad Sci USA 92:10555-10559
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10555-10559
    • Lodmell, J.S.1    Gutell, R.R.2    Dahlberg, A.E.3
  • 59
    • 0027441282 scopus 로고
    • The 5' proximal helix of 16S rRNA is involved in the binding of streptomycin to the ribosome
    • Pinard R, Payant C, Melancon P, Brakier-Gingras L (1993) The 5' proximal helix of 16S rRNA is involved in the binding of streptomycin to the ribosome. FASEB J 7:173-176
    • (1993) FASEB J , vol.7 , pp. 173-176
    • Pinard, R.1    Payant, C.2    Melancon, P.3    Brakier-Gingras, L.4
  • 60
    • 0025799516 scopus 로고
    • A single base substitution in 16S ribosomal RNA suppresses streptomycin dependence and increases the frequency of translational Errors
    • Allen PN, Noller HF (1991) A single base substitution in 16S ribosomal RNA suppresses streptomycin dependence and increases the frequency of translational Errors. Cell 66:141-148
    • (1991) Cell , vol.66 , pp. 141-148
    • Allen, P.N.1    Noller, H.F.2
  • 61
    • 0015937147 scopus 로고
    • Colicin E3 induced cleavage of 16S ribosomal RNA; blocking effects of certain antibiotics
    • Dahlberg AE, Lund E, Kjeldgaard NO, Bowman CM, Nomura M (1973) Colicin E3 induced cleavage of 16S ribosomal RNA; blocking effects of certain antibiotics. Biochemistry 12:948-950
    • (1973) Biochemistry , vol.12 , pp. 948-950
    • Dahlberg, A.E.1    Lund, E.2    Kjeldgaard, N.O.3    Bowman, C.M.4    Nomura, M.5
  • 62
    • 0023689711 scopus 로고
    • A mutation in the 530 loop of Escherichia coli 16S ribosomal RNA causes resistance to streptomycin
    • Melançon P, Lemieux C, Brakier-Gingras L (1988) A mutation in the 530 loop of Escherichia coli 16S ribosomal RNA causes resistance to streptomycin. Nucleic Acids Res 16: 9631-9639
    • (1988) Nucleic Acids Res , vol.16 , pp. 9631-9639
    • Melançon, P.1    Lemieux, C.2    Brakier-Gingras, L.3
  • 63
    • 0025737972 scopus 로고
    • A functional pseudoknot in 16S ribosomal RNA
    • Powers T, Noller HF (1991) A functional pseudoknot in 16S ribosomal RNA. EMBO J 10:2203-2214
    • (1991) EMBO J , vol.10 , pp. 2203-2214
    • Powers, T.1    Noller, H.F.2
  • 64
    • 0026764788 scopus 로고
    • Structure-function correlations (and discrepancies) in the 16S ribosomal RNA from Escherichia coli
    • Brimacombe R (1992) Structure-function correlations (and discrepancies) in the 16S ribosomal RNA from Escherichia coli. Biochimie 74:319-326
    • (1992) Biochimie , vol.74 , pp. 319-326
    • Brimacombe, R.1
  • 65
    • 0024344098 scopus 로고
    • RNA-protein interactions in 30S ribosomal subunits: Folding and function of 16S rRNA
    • Stern S, Powers T, Changchien LM, Noller HF (1989) RNA-protein interactions in 30S ribosomal subunits: folding and function of 16S rRNA. Science 244:783-790
    • (1989) Science , vol.244 , pp. 783-790
    • Stern, S.1    Powers, T.2    Changchien, L.M.3    Noller, H.F.4
  • 66
    • 0029286628 scopus 로고
    • Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA
    • Powers T, Noller HF (1995) Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA. RNA 1:194-209
    • (1995) RNA , vol.1 , pp. 194-209
    • Powers, T.1    Noller, H.F.2
  • 67
    • 0023091436 scopus 로고
    • Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides
    • Beauclerk AAD, Cundliffe E (1987) Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides. J Mol Biol 193:661-671
    • (1987) J Mol Biol , vol.193 , pp. 661-671
    • Beauclerk, A.A.D.1    Cundliffe, E.2
  • 68
    • 0021892944 scopus 로고
    • The nucleotide sequence of the 17S ribosomal RNA gene of Tetrahymena rhermophilia and the identification of point mutations resulting in resistance to the antibiotics paromomycin and hygromycin
    • Spangler EA, Blackburn EH (1985) The nucleotide sequence of the 17S ribosomal RNA gene of Tetrahymena rhermophilia and the identification of point mutations resulting in resistance to the antibiotics paromomycin and hygromycin. J Biol Chem 260:6334-6340
    • (1985) J Biol Chem , vol.260 , pp. 6334-6340
    • Spangler, E.A.1    Blackburn, E.H.2
  • 69
    • 0024424033 scopus 로고
    • Mutations in 16S ribosomal RNA disrupt antibiotic-RNA interaction
    • De Stasio EA, Moazed D, Noller HF, Dahlberg AE (1989) Mutations in 16S ribosomal RNA disrupt antibiotic-RNA interaction. EMBO J 8:1213-1216
    • (1989) EMBO J , vol.8 , pp. 1213-1216
    • De Stasio, E.A.1    Moazed, D.2    Noller, H.F.3    Dahlberg, A.E.4
  • 70
    • 0025305692 scopus 로고
    • Effects of mutagenesis of a conserved base-paired site near the decoding region of Escherichia coli 16S ribosomal RNA
    • De Stasio EA, Dahlberg AE (1990) Effects of mutagenesis of a conserved base-paired site near the decoding region of Escherichia coli 16S ribosomal RNA. J Mol Biol 212:127-133
    • (1990) J Mol Biol , vol.212 , pp. 127-133
    • De Stasio, E.A.1    Dahlberg, A.E.2
  • 71
    • 0026322432 scopus 로고
    • Interaction between 16S ribosomal RNA and ribosomal protein S12: Differential effects of paromomycin and streptomycin
    • O'Connor M, De Stasio EA, Dahlberg AE (1991) Interaction between 16S ribosomal RNA and ribosomal protein S12: differential effects of paromomycin and streptomycin. Biochimie 73:1493-1500
    • (1991) Biochimie , vol.73 , pp. 1493-1500
    • O'Connor, M.1    De Stasio, E.A.2    Dahlberg, A.E.3
  • 72
    • 0024420980 scopus 로고
    • Mutations in ribosomal proteins S4 and S12 influence the higher-order structure of 16S ribosomal RNA
    • Allen PN, Noller HF (1989) Mutations in ribosomal proteins S4 and S12 influence the higher-order structure of 16S ribosomal RNA. J Mol Biol 208:457-168
    • (1989) J Mol Biol , vol.208 , pp. 457-1168
    • Allen, P.N.1    Noller, H.F.2
  • 73
    • 0017188238 scopus 로고
    • Paromomycin and dihydrostreptomycin bind to Escherichia coli ribosomes
    • Lando D, Cousin AM, Ojasoo T, Raynaud JP (1976) Paromomycin and dihydrostreptomycin bind to Escherichia coli ribosomes. Eur J Biochem 66:597-606
    • (1976) Eur J Biochem , vol.66 , pp. 597-606
    • Lando, D.1    Cousin, A.M.2    Ojasoo, T.3    Raynaud, J.P.4
  • 74
    • 0018078433 scopus 로고
    • Interaction of kanamycin and related antibiotics with the large subunit of ribosomes and the inhibition of translocation
    • Misumi M, Nishimura T, Komai T, Tanaka N (1978) Interaction of kanamycin and related antibiotics with the large subunit of ribosomes and the inhibition of translocation. Biochem Biophys Res Commun 84:358-365
    • (1978) Biochem Biophys Res Commun , vol.84 , pp. 358-365
    • Misumi, M.1    Nishimura, T.2    Komai, T.3    Tanaka, N.4
  • 75
    • 0020583413 scopus 로고
    • The inhibition pattern of antibiotics on the extent and accuracy of tRNA binding to the ribosome and their effect on the subsequent steps in chain elongation
    • Wurmbach P, Nierhaus KH (1983) The inhibition pattern of antibiotics on the extent and accuracy of tRNA binding to the ribosome and their effect on the subsequent steps in chain elongation. Eur J Biochem 130:9-12
    • (1983) Eur J Biochem , vol.130 , pp. 9-12
    • Wurmbach, P.1    Nierhaus, K.H.2
  • 76
    • 0001874236 scopus 로고
    • Structure, Function, and Evolution of Mammalian Ribosomes
    • Hill WE, Dahlberg A. Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) American Society for Microbiology, Washington
    • Wool IG, Endo Y, Chan Y-L, Glück A (1990) Structure, Function, and Evolution of Mammalian Ribosomes. In: Hill WE, Dahlberg A. Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) The ribosome, structure function and evolution. American Society for Microbiology, Washington, pp 203-214
    • (1990) The Ribosome, Structure Function and Evolution , pp. 203-214
    • Wool, I.G.1    Endo, Y.2    Chan, Y.-L.3    Glück, A.4
  • 77
    • 0023405923 scopus 로고
    • Evidence that the G2661 region of the 23S rRNA is located at the ribosomal binding sites of both elongation factors
    • Hausner TP, Atmadja J, Nierhaus KH (1987) Evidence that the G2661 region of the 23S rRNA is located at the ribosomal binding sites of both elongation factors. Biochimie 69:911-923
    • (1987) Biochimie , vol.69 , pp. 911-923
    • Hausner, T.P.1    Atmadja, J.2    Nierhaus, K.H.3
  • 78
    • 0023722010 scopus 로고
    • Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S rRNA
    • Moazed D, Robertson JM, Noller HF (1988) Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S rRNA. Nature 334:362-364
    • (1988) Nature , vol.334 , pp. 362-364
    • Moazed, D.1    Robertson, J.M.2    Noller, H.F.3
  • 79
    • 0021781999 scopus 로고
    • Mechanism of action of kirromycin-like antibiotics
    • Parmeggiani A, Swart GWM (1985) Mechanism of action of kirromycin-like antibiotics. Annu Rev Microbiol 39:557-577
    • (1985) Annu Rev Microbiol , vol.39 , pp. 557-577
    • Parmeggiani, A.1    Swart, G.W.M.2
  • 81
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard M, Nissen P, Thirup S, Nyborg J (1993) The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure 1:35-50
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 82
    • 0028000039 scopus 로고
    • The structural and functional basis for the kirromycin resistance of minant EF-Tu species in Escherichia coli
    • Mesters JR, Zeef LAH, Hilgenfeld R, de Graaf JM, Kraal B, Bosch L (1994) The structural and functional basis for the kirromycin resistance of minant EF-Tu species in Escherichia coli. EMBO J 13:4877-4885
    • (1994) EMBO J , vol.13 , pp. 4877-4885
    • Mesters, J.R.1    Zeef, L.A.H.2    Hilgenfeld, R.3    De Graaf, J.M.4    Kraal, B.5    Bosch, L.6
  • 85
    • 0029006133 scopus 로고
    • Codon-dependent conformational change of elongation factor Tu preceding OTP hydrolysis on the ribosome
    • Rodnina MV, Fricke R, Kuhn L, Wintermeyer W (1995) Codon-dependent conformational change of elongation factor Tu preceding OTP hydrolysis on the ribosome. EMBO J 14:2613-2619
    • (1995) EMBO J , vol.14 , pp. 2613-2619
    • Rodnina, M.V.1    Fricke, R.2    Kuhn, L.3    Wintermeyer, W.4
  • 86
    • 0025866195 scopus 로고
    • Mutant ribosomes can generate dominant kirromycin resistance
    • Tubulekas I, Buckingham RH, Hughes D (1991) Mutant ribosomes can generate dominant kirromycin resistance. J Bacteriol 173:3635-3643
    • (1991) J Bacteriol , vol.173 , pp. 3635-3643
    • Tubulekas, I.1    Buckingham, R.H.2    Hughes, D.3
  • 87
    • 0013508244 scopus 로고
    • Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA
    • Wolf H, Assmann D, Fischer E (1978) Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA. Proc Natl Acad Sci USA 75:5324-5328
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5324-5328
    • Wolf, H.1    Assmann, D.2    Fischer, E.3
  • 89
    • 0026030903 scopus 로고
    • New antibiotic that acts specifically on the GTP-bound form of elongation factor Tu
    • Anborgh PH, Parmeggiani A (1991) New antibiotic that acts specifically on the GTP-bound form of elongation factor Tu. EMBO J 10:779-784
    • (1991) EMBO J , vol.10 , pp. 779-784
    • Anborgh, P.H.1    Parmeggiani, A.2
  • 90
    • 0020341129 scopus 로고
    • Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity
    • Schulze H, Nierhaus KH (1982) Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity. EMBO J 1:609-613
    • (1982) EMBO J , vol.1 , pp. 609-613
    • Schulze, H.1    Nierhaus, K.H.2
  • 91
    • 0025051302 scopus 로고
    • Ribosomal proteins L15 and L16 are mere late assembly proteins of the large ribosomal subunit
    • Franceschi FJ, Nierhaus KH (1990) Ribosomal proteins L15 and L16 are mere late assembly proteins of the large ribosomal subunit. J Biol Chem 265:16676-16682
    • (1990) J Biol Chem , vol.265 , pp. 16676-16682
    • Franceschi, F.J.1    Nierhaus, K.H.2
  • 92
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction procedures
    • Noller HF, Hoffarth V, Zimniak L (1992) Unusual resistance of peptidyl transferase to protein extraction procedures. Science 256:1416-1419
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 93
    • 0027247953 scopus 로고
    • Peptidyl transferase: Protein, ribonucleo-protein, or RNA?
    • Noller HF (1993) Peptidyl transferase: protein, ribonucleo-protein, or RNA? J Bacteriol 175:5297-5300
    • (1993) J Bacteriol , vol.175 , pp. 5297-5300
    • Noller, H.F.1
  • 94
    • 0003053221 scopus 로고
    • Antibiotic probes of Escherichia coli ribosomal peptidyltransferase
    • Hill WE, Dahlberg A, Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) American Society for Microbiology, Washington
    • Cooperman BS, Weitzman CJ, Fernández CL (1990) Antibiotic probes of Escherichia coli ribosomal peptidyltransferase. In: Hill WE, Dahlberg A, Garrett RA, Moore PM, Schlessinger D, Warner JR (eds) The ribosome, structure function and evolution. American Society for Microbiology, Washington, pp 479-490
    • (1990) The Ribosome, Structure Function and Evolution , pp. 479-490
    • Cooperman, B.S.1    Weitzman, C.J.2    Fernández, C.L.3
  • 95
    • 0029085929 scopus 로고
    • A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome
    • Samaha RR, Green R, Noller HF (1995) A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome. Nature 377:309-314
    • (1995) Nature , vol.377 , pp. 309-314
    • Samaha, R.R.1    Green, R.2    Noller, H.F.3
  • 96
    • 0028924641 scopus 로고
    • Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic ribosome complexes
    • Rodriguez-Fonseca C, Amilis R, Garrett RA (1995) Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic ribosome complexes. J Mol Biol 247:224-235
    • (1995) J Mol Biol , vol.247 , pp. 224-235
    • Rodriguez-Fonseca, C.1    Amilis, R.2    Garrett, R.A.3
  • 97
    • 0024114860 scopus 로고
    • The importance of highly conserved nucleotides in the binding region of chloramphenicol at the peptidyl transfer centre of Escherichia coli 23S ribosomal RNA
    • Vester B, Garrett RA (1988) The importance of highly conserved nucleotides in the binding region of chloramphenicol at the peptidyl transfer centre of Escherichia coli 23S ribosomal RNA. EMBO J 7:3577-3587
    • (1988) EMBO J , vol.7 , pp. 3577-3587
    • Vester, B.1    Garrett, R.A.2
  • 98
    • 0025151914 scopus 로고
    • Partial release of AcPhe-Phe-tRNA from ribosomes during poly(U)-dependent poly(Phe) synthesis and the effects of chloramphenicol
    • Rheinberger HJ, Nierhaus KH (1990) Partial release of AcPhe-Phe-tRNA from ribosomes during poly(U)-dependent poly(Phe) synthesis and the effects of chloramphenicol. Eur J Biochem 193:643-650
    • (1990) Eur J Biochem , vol.193 , pp. 643-650
    • Rheinberger, H.J.1    Nierhaus, K.H.2
  • 99
    • 0020322533 scopus 로고
    • Erythromycin, carbomycin, and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes
    • Menninger JR, Otto DP (1982) Erythromycin, carbomycin, and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes. Antimicrob Agents Chemother 21:810-818.
    • (1982) Antimicrob Agents Chemother , vol.21 , pp. 810-818
    • Menninger, J.R.1    Otto, D.P.2
  • 100
    • 0023604799 scopus 로고
    • Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA
    • Moazed D, Noller HF (1987) Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA. Biochimie 69:879-884
    • (1987) Biochimie , vol.69 , pp. 879-884
    • Moazed, D.1    Noller, H.F.2
  • 101
    • 0026771498 scopus 로고
    • Novel mutants of 23S RNA: Characterization of functional properties
    • Saarma U, Remme J (1992) Novel mutants of 23S RNA: characterization of functional properties. Nucleic Acids Res 20:3147-3152
    • (1992) Nucleic Acids Res , vol.20 , pp. 3147-3152
    • Saarma, U.1    Remme, J.2
  • 102
    • 0026601409 scopus 로고
    • Functional Interactions within 23S rRNA Involving the Peptidyltransferase Center
    • Douthwaite S (1992) Functional Interactions within 23S rRNA Involving the Peptidyltransferase Center. J Bacteriol 174:1333-1338
    • (1992) J Bacteriol , vol.174 , pp. 1333-1338
    • Douthwaite, S.1
  • 103
    • 0015831640 scopus 로고
    • Identification of the chloramphenicol-binding protein in Escherichia coli ribosomes by partial reconstitution
    • Nierhaus D, Nierhaus KH (1973) Identification of the chloramphenicol-binding protein in Escherichia coli ribosomes by partial reconstitution. Proc Natl Acad Sci USA 70:2224-2228
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 2224-2228
    • Nierhaus, D.1    Nierhaus, K.H.2
  • 104
    • 0027493781 scopus 로고
    • Interaction between the antibiotic spiramycin and a ribosonial complex active in peptide bond formation
    • Dinos G, Synctos D, Coutsogeorgopoulos C (1993) Interaction between the antibiotic spiramycin and a ribosonial complex active in peptide bond formation. Biochemistry 32:10638-10647
    • (1993) Biochemistry , vol.32 , pp. 10638-10647
    • Dinos, G.1    Synctos, D.2    Coutsogeorgopoulos, C.3
  • 105
    • 0027234428 scopus 로고
    • Lincosamide antibiotics stimulate dissociation of peptidyl-tRNA from rihosomes
    • Menninger JR, Coleman RA (1993) Lincosamide antibiotics stimulate dissociation of peptidyl-tRNA from rihosomes. Antimicrob Agents Chemother 37:2027-2029
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 2027-2029
    • Menninger, J.R.1    Coleman, R.A.2
  • 106
    • 0023949497 scopus 로고
    • Protein components of the erythrotmcin binding site in bacterial ribosomes
    • Arevalo MA, Tejedor F, Polo F, Ballesta JP (1988) Protein components of the erythrotmcin binding site in bacterial ribosomes. J Biol Chem 263:58-63
    • (1988) J Biol Chem , vol.263 , pp. 58-63
    • Arevalo, M.A.1    Tejedor, F.2    Polo, F.3    Ballesta, J.P.4
  • 107
    • 0026660662 scopus 로고
    • Interaction of the antibiotics clindamycin and lincomycin with Escherichia coli 23S ribosomal RNA
    • Douthwaite S (1992) Interaction of the antibiotics clindamycin and lincomycin with Escherichia coli 23S ribosomal RNA. Nucleic Acids Res 20:4717-4720
    • (1992) Nucleic Acids Res , vol.20 , pp. 4717-4720
    • Douthwaite, S.1
  • 108
    • 0027248565 scopus 로고
    • Erythromycin binding is reduced in ribosomes with conformational alterations in the 23 S rRNA peptidyl transferase Loop
    • Douthwaite S, Aagaard C (1993) Erythromycin binding is reduced in ribosomes with conformational alterations in the 23 S rRNA peptidyl transferase Loop. J Mol Biol 232:725-731
    • (1993) J Mol Biol , vol.232 , pp. 725-731
    • Douthwaite, S.1    Aagaard, C.2
  • 109
    • 0018197197 scopus 로고
    • Proteins from Esherichia coli ribosomes involved in binding of erythromycin
    • Teraoka H, Nierhaus KH (1978) Proteins from Esherichia coli ribosomes involved in binding of erythromycin. J Mol Biol 126:185-193
    • (1978) J Mol Biol , vol.126 , pp. 185-193
    • Teraoka, H.1    Nierhaus, K.H.2
  • 110
    • 0021016454 scopus 로고
    • Characterisation of a mutant from Escherichia coli lacking protein L15 and localisation of protein L15 by immuno-electron microscopy
    • Lotti M, Dabbs ER, Hasenbank R, Stöffler-Meilike M, Stöffler G (1983) Characterisation of a mutant from Escherichia coli lacking protein L15 and localisation of protein L15 by immuno-electron microscopy. Mol Gen Genet 192:295-300
    • (1983) Mol Gen Genet , vol.192 , pp. 295-300
    • Lotti, M.1    Dabbs, E.R.2    Hasenbank, R.3    Stöffler-Meilike, M.4    Stöffler, G.5
  • 111
    • 0028148698 scopus 로고
    • Ribosonial protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli
    • Chittum HS, Champney WS (1994) Ribosonial protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli. J Bacteriol 176:6192-6198
    • (1994) J Bacteriol , vol.176 , pp. 6192-6198
    • Chittum, H.S.1    Champney, W.S.2
  • 112
    • 0022851263 scopus 로고
    • Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site components
    • Tejedor F, Ballesta JPG (1986) Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site components. Biochemistry 25:7725-7731
    • (1986) Biochemistry , vol.25 , pp. 7725-7731
    • Tejedor, F.1    Ballesta, J.P.G.2
  • 113
    • 0017897566 scopus 로고
    • Characterisation of the binding of Virginiamycin S to Escherichia coli ribosomes
    • de Bethune M-P, Nierhaus KH (1978) Characterisation of the binding of Virginiamycin S to Escherichia coli ribosomes. Eur J Biochem 86: 187-191
    • (1978) Eur J Biochem , vol.86 , pp. 187-191
    • De Bethune, M.-P.1    Nierhaus, K.H.2
  • 114
    • 0025090786 scopus 로고
    • Affinity labeling of the virginiamycin S binding site on bacterial ribosome
    • Di Giambattista M, Nyssen E, Pecher A, Cocito C (1990) Affinity labeling of the virginiamycin S binding site on bacterial ribosome. Biochemistry 9:9203-9211
    • (1990) Biochemistry , vol.9 , pp. 9203-9211
    • Di Giambattista, M.1    Nyssen, E.2    Pecher, A.3    Cocito, C.4
  • 115
    • 0028099297 scopus 로고
    • Chemical probing of a virginiamycin M-promoted conformational change of the peptidyl-transferase domain
    • Vannuffel P, Di Giambattisla M, Cocito C (1994) Chemical probing of a virginiamycin M-promoted conformational change of the peptidyl-transferase domain. Nucleic Acids Res 22:4449-4453
    • (1994) Nucleic Acids Res , vol.22 , pp. 4449-4453
    • Vannuffel, P.1    Di Giambattisla, M.2    Cocito, C.3
  • 116
    • 0026671180 scopus 로고
    • The role of rRNA bases in the interaction of peptidyltransferase inhibitors with bacterial ribosomes
    • Vannuffel P, Di Giambattisla M, Cocito C (1992) The role of rRNA bases in the interaction of peptidyltransferase inhibitors with bacterial ribosomes. J Biol Chem 267:16114-16120
    • (1992) J Biol Chem , vol.267 , pp. 16114-16120
    • Vannuffel, P.1    Di Giambattisla, M.2    Cocito, C.3
  • 117
    • 0021112383 scopus 로고
    • Chemical crosslinking of elongation factor G to the 23S rRNA in 70S ribosomes from Escherichia coli
    • Sköld SE (1983) Chemical crosslinking of elongation factor G to the 23S rRNA in 70S ribosomes from Escherichia coli. Nucleic Acids Res 11:4923-4932
    • (1983) Nucleic Acids Res , vol.11 , pp. 4923-4932
    • Sköld, S.E.1
  • 118
    • 0025907657 scopus 로고
    • α-Sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome
    • Miller SP, Bodley JW (1991) α-Sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome. Nucleic Acids Res 19:1657-1660
    • (1991) Nucleic Acids Res , vol.19 , pp. 1657-1660
    • Miller, S.P.1    Bodley, J.W.2
  • 119
    • 0028134851 scopus 로고
    • Cross-hypersensitivity effects of mutations in 23 S rRNA yield insight into aminoacyl-tRNA binding
    • Mankin AS, Leviev I, Garrett RA (1994) Cross-hypersensitivity effects of mutations in 23 S rRNA yield insight into aminoacyl-tRNA binding. J Mol Biol 244:151-157
    • (1994) J Mol Biol , vol.244 , pp. 151-157
    • Mankin, A.S.1    Leviev, I.2    Garrett, R.A.3
  • 120
    • 0024349978 scopus 로고
    • Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23S rRNA
    • Egebjerg J, Douthwaite S, Garrett RA (1989) Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23S rRNA. EMBO J 8:607-611
    • (1989) EMBO J , vol.8 , pp. 607-611
    • Egebjerg, J.1    Douthwaite, S.2    Garrett, R.A.3
  • 121
    • 0025330496 scopus 로고
    • 4 pentameric complex in the GTPase domain of 23 S ribosonial RNA from Escherichia coli
    • 4 pentameric complex in the GTPase domain of 23 S ribosonial RNA from Escherichia coli. J Mol Biol 213:275-288
    • (1990) J Mol Biol , vol.213 , pp. 275-288
    • Egebjerg, J.1    Douthwaite, S.2    Liljas, A.3    Garrett, R.A.4
  • 122
    • 0025999688 scopus 로고
    • Recognition of the highly conserved GTPase center of 23 S ribosonial RNA by ribosonial protein L11 and the antibiotic thiostrepton
    • Ryan PC, Lu M, Draper DE (1991) Recognition of the highly conserved GTPase center of 23 S ribosonial RNA by ribosonial protein L11 and the antibiotic thiostrepton. J Mol Biol 221:1257-1268
    • (1991) J Mol Biol , vol.221 , pp. 1257-1268
    • Ryan, P.C.1    Lu, M.2    Draper, D.E.3
  • 123
    • 0027732617 scopus 로고
    • 4 and he antibiotic thiostrepton interact with overlapping regions of the 23 S rRNA backbone in the ribosomal GTPase centre
    • 4 and (he antibiotic thiostrepton interact with overlapping regions of the 23 S rRNA backbone in the ribosomal GTPase centre. J Mol Biol 234:1013-1020
    • (1993) J Mol Biol , vol.234 , pp. 1013-1020
    • Rosendahl, G.1    Douthwait, S.2
  • 124
    • 0023689001 scopus 로고
    • Site-directed mutagenesis of Escherichia coli 23 S ribosomal RNA at position 1067 within the GTP hydrolysis centre
    • Thompson J, Cundliffe E, Dahlberg AE (1988) Site-directed mutagenesis of Escherichia coli 23 S ribosomal RNA at position 1067 within the GTP hydrolysis centre. J Mol Biol 203:457-465
    • (1988) J Mol Biol , vol.203 , pp. 457-465
    • Thompson, J.1    Cundliffe, E.2    Dahlberg, A.E.3
  • 125
    • 0028355760 scopus 로고
    • The antibiotics micrococcin and thiostrepton interact directely with 23S rRNA nucleotides 1067A and 1095A
    • Rosendahl G, Douthwaite S (1994) The antibiotics micrococcin and thiostrepton interact directely with 23S rRNA nucleotides 1067A and 1095A. Nucleic Acids Res 22:357-363
    • (1994) Nucleic Acids Res , vol.22 , pp. 357-363
    • Rosendahl, G.1    Douthwaite, S.2
  • 126
    • 0027480627 scopus 로고
    • Replacement of the L11 binding region within E. coli 23S ribosomal RNA with ist homologue from yeast: In vivo and in vitro analysis of hybrid ribosomes altered in the GTPase centre
    • Thompson J, Musters W, Cundliffe E, Dahlberg AE (1993) Replacement of the L11 binding region within E. coli 23S ribosomal RNA with ist homologue from yeast: in vivo and in vitro analysis of hybrid ribosomes altered in the GTPase centre. EMBO J 12:1499-1504
    • (1993) EMBO J , vol.12 , pp. 1499-1504
    • Thompson, J.1    Musters, W.2    Cundliffe, E.3    Dahlberg, A.E.4
  • 127
    • 0029585980 scopus 로고
    • A base substitution within the GTPase-associated domain of mammalian 28 S ribosomal RNA causes high thiostrepton accessibility
    • Uchiumi T, Wada A, Kominami R (1995) A base substitution within the GTPase-associated domain of mammalian 28 S ribosomal RNA causes high thiostrepton accessibility. J Biol Chem 270:29889-29893
    • (1995) J Biol Chem , vol.270 , pp. 29889-29893
    • Uchiumi, T.1    Wada, A.2    Kominami, R.3
  • 128
    • 0026005654 scopus 로고
    • The binding of thiostrepton to 23S ribosomal RNA
    • Thompson J, Cundliffe E (1991) The binding of thiostrepton to 23S ribosomal RNA. Biochimie 73:1131-1135
    • (1991) Biochimie , vol.73 , pp. 1131-1135
    • Thompson, J.1    Cundliffe, E.2
  • 129
    • 0025807847 scopus 로고
    • Detection of a tertiary interaction in the highly conserved GTPase center of large subunit ribosomal RNA
    • Ryan PC, Draper DE (1991) Detection of a tertiary interaction in the highly conserved GTPase center of large subunit ribosomal RNA. Proc Natl Acad Sci USA 88:6308-6312
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6308-6312
    • Ryan, P.C.1    Draper, D.E.2
  • 130
    • 0002241318 scopus 로고
    • Involvement of specific portions of ribosomal RNA in defined ribosoamal functions: A study utilizing antibiotics
    • Hardesty B, Kramer G (eds) Springer, Berlin Heidelberg New York
    • Cundliffe E (1986) Involvement of specific portions of ribosomal RNA in defined ribosoamal functions: a study utilizing antibiotics. In: Hardesty B, Kramer G (eds) Structure, function, and genetics of ribosomes. Springer, Berlin Heidelberg New York, pp 586-604
    • (1986) Structure, Function, and Genetics of Ribosomes , pp. 586-604
    • Cundliffe, E.1
  • 131
    • 0029044463 scopus 로고
    • Thermodynamics of RNA unfolding: Stabilization of a ribosomal RNA tertiary structure by thiostrepton and ammonium Ion
    • Draper DE, Xing Y, Laing LG (1995) Thermodynamics of RNA unfolding: stabilization of a ribosomal RNA tertiary structure by thiostrepton and ammonium Ion. J Mol Biol 249:231-238
    • (1995) J Mol Biol , vol.249 , pp. 231-238
    • Draper, D.E.1    Xing, Y.2    Laing, L.G.3
  • 132
    • 0025039610 scopus 로고
    • Similarities and differences in the inhibition patterns of thiostrepton and viomycin: Evidence for two functionally different populations of P sites when occupied with AcPhe-tRNA
    • Kutay UR, Spahn CMT, Nierhaus KH (1990) Similarities and differences in the inhibition patterns of thiostrepton and viomycin: evidence for two functionally different populations of P sites when occupied with AcPhe-tRNA. Biochim Biophys Acta 1050:193-196
    • (1990) Biochim Biophys Acta , vol.1050 , pp. 193-196
    • Kutay, U.R.1    Spahn, C.M.T.2    Nierhaus, K.H.3
  • 133
    • 0018165088 scopus 로고
    • Resistance to viomycin conferred by RNA of either ribosomal subunit
    • Yamada T, Mizugichi Y, Nierhaus KH, Wittmann HG (1978) Resistance to viomycin conferred by RNA of either ribosomal subunit. Nature 275:460-461
    • (1978) Nature , vol.275 , pp. 460-461
    • Yamada, T.1    Mizugichi, Y.2    Nierhaus, K.H.3    Wittmann, H.G.4
  • 134
    • 0028090796 scopus 로고
    • Selective perturbation of G530 of 16 S rRNA by translational miscoding agents and a streptomycin-dependence mutation in Protein S12
    • Powers T, Noller HF (1994) Selective perturbation of G530 of 16 S rRNA by translational miscoding agents and a streptomycin-dependence mutation in Protein S12. J Mol Biol 235:156-172
    • (1994) J Mol Biol , vol.235 , pp. 156-172
    • Powers, T.1    Noller, H.F.2
  • 135
    • 0017818857 scopus 로고
    • Viomycin favours the formation of 70S ribosome couples
    • Yamada T, Nierhaus KH (1978) Viomycin favours the formation of 70S ribosome couples. Mol Gen Genet 161:261-265
    • (1978) Mol Gen Genet , vol.161 , pp. 261-265
    • Yamada, T.1    Nierhaus, K.H.2
  • 137
    • 0016679542 scopus 로고
    • Genetic position and amino acid replacements of several mutations in ribosomal protein S5 from Escherichia coli
    • Piepersberg W, Bock A, Yaguchi M, Wittmann HG (1975) Genetic position and amino acid replacements of several mutations in ribosomal protein S5 from Escherichia coli. Mol Gen Genet 143:43-52
    • (1975) Mol Gen Genet , vol.143 , pp. 43-52
    • Piepersberg, W.1    Bock, A.2    Yaguchi, M.3    Wittmann, H.G.4
  • 138
    • 0021760461 scopus 로고
    • Antibiotic resistance mutations in 16S and 23S ribosomal RNA genes of AV cherichia coli
    • Sigmund C, Ettayebi M, Morgan E (1984) Antibiotic resistance mutations in 16S and 23S ribosomal RNA genes of AV cherichia coli. Nucleic Acids Res 12:4653-1663
    • (1984) Nucleic Acids Res , vol.12 , pp. 4653-11663
    • Sigmund, C.1    Ettayebi, M.2    Morgan, E.3
  • 139
    • 0023604801 scopus 로고
    • Spectinomycin resistance at site 1192 in 16S ribosomal RNA of E. coli: An analysis of three mutants
    • Makosky PC, Dahlberg AE (1987) Spectinomycin resistance at site 1192 in 16S ribosomal RNA of E. coli: an analysis of three mutants. Biochimie 69:885-889
    • (1987) Biochimie , vol.69 , pp. 885-889
    • Makosky, P.C.1    Dahlberg, A.E.2
  • 140
    • 0028359389 scopus 로고
    • Spectinomycin interacts specifically with the residues G1064 and C1192 in 16S rRNA, thereby potentially freezing this molecule into an inactive conformation
    • Brink MF, Brink G, Verbeet MP, de Boer HA (1994) Spectinomycin interacts specifically with the residues G1064 and C1192 in 16S rRNA, thereby potentially freezing this molecule into an inactive conformation. Nucleic Acids Res 22:325-331
    • (1994) Nucleic Acids Res , vol.22 , pp. 325-331
    • Brink, M.F.1    Brink, G.2    Verbeet, M.P.3    De Boer, H.A.4
  • 141
    • 0028944493 scopus 로고
    • A new mutation in 16S rRNA of Escherichia coli conferring spectinomycin resistance
    • Johanson U, Hughes D (1995) A new mutation in 16S rRNA of Escherichia coli conferring spectinomycin resistance. Nucleic Acids Res 23:464-466
    • (1995) Nucleic Acids Res , vol.23 , pp. 464-466
    • Johanson, U.1    Hughes, D.2
  • 142
    • 0027979072 scopus 로고
    • Independent in vitro assembly of a ribonucleoprotein particle containing the 3′ domain of 16S rRNA
    • Samaha RR, O'Brien B, O'Brien TW, Noller HF (1994) Independent in vitro assembly of a ribonucleoprotein particle containing the 3′ domain of 16S rRNA. Proc Natl Acad Sci USA 91:7884-7888
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7884-7888
    • Samaha, R.R.1    O'Brien, B.2    O'Brien, T.W.3    Noller, H.F.4
  • 143
    • 0026687213 scopus 로고
    • The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA
    • Ramakrishnan V, White SW (1992) The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA. Nature 358:768-771
    • (1992) Nature , vol.358 , pp. 768-771
    • Ramakrishnan, V.1    White, S.W.2
  • 144
    • 0026535291 scopus 로고
    • Mutations in E. coli 16S rR-NA that enhance and decrease the activity of a suppressor tRNA
    • Prescott CD, Kornau HC (1992) Mutations in E. coli 16S rR-NA that enhance and decrease the activity of a suppressor tRNA. Nucleic Acids Res 20:1567-1571
    • (1992) Nucleic Acids Res , vol.20 , pp. 1567-1571
    • Prescott, C.D.1    Kornau, H.C.2
  • 145
    • 0027988206 scopus 로고
    • Mutations in helix 34 of Escherichia coli 16S ribosomal RNA have multiple effects on ribosome function and synthesis
    • Moine H, Dahlberg AE (1994) Mutations in helix 34 of Escherichia coli 16S ribosomal RNA have multiple effects on ribosome function and synthesis. J Mol Biol 243:402-412
    • (1994) J Mol Biol , vol.243 , pp. 402-412
    • Moine, H.1    Dahlberg, A.E.2
  • 146
    • 0016737059 scopus 로고
    • Some characteristics of and structural requirements for the interaction of 24, 25-dihydrofusidic acid with ribosome elongation factor G complexes
    • Willie GR, Richman N, Godfredsen WO, Bodley JW (1975) Some characteristics of and structural requirements for the interaction of 24, 25-dihydrofusidic acid with ribosome elongation factor G complexes. Biochemistry 14:1713-1718
    • (1975) Biochemistry , vol.14 , pp. 1713-1718
    • Willie, G.R.1    Richman, N.2    Godfredsen, W.O.3    Bodley, J.W.4
  • 147
    • 0028214276 scopus 로고
    • Fusidic acid-resistant mutations define three regions in elongation factor G of Salmonella typhimurium
    • Johanson U, Hughes D (1994) Fusidic acid-resistant mutations define three regions in elongation factor G of Salmonella typhimurium. Gene 143:55-59
    • (1994) Gene , vol.143 , pp. 55-59
    • Johanson, U.1    Hughes, D.2
  • 148
    • 0025873818 scopus 로고
    • Antibiotic inhibition of group I ribozyme function
    • von Ahsen U, Davies J, Schroeder R (1993) Antibiotic inhibition of group I ribozyme function. Nature 1993:368-370
    • (1993) Nature , vol.1993 , pp. 368-370
    • Von Ahsen, U.1    Davies, J.2    Schroeder, R.3
  • 149
    • 0029258393 scopus 로고
    • Inhibition of the hammerhead ribozyme by neomycin
    • Stage TK, Hertel KJ, Uhlenbeck OC (1995) Inhibition of the hammerhead ribozyme by neomycin. RNA 1:95-101
    • (1995) RNA , vol.1 , pp. 95-101
    • Stage, T.K.1    Hertel, K.J.2    Uhlenbeck, O.C.3
  • 150
    • 0027370433 scopus 로고
    • Small molecules that selectively block RNA binding of HIV-I Rev protein inhibit Rev function and viral production
    • Zapp ML, Stern S, Green MR (1993) Small molecules that selectively block RNA binding of HIV-I Rev protein inhibit Rev function and viral production. Cell 74:969-978
    • (1993) Cell , vol.74 , pp. 969-978
    • Zapp, M.L.1    Stern, S.2    Green, M.R.3


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