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Volumn 259, Issue 1, 1996, Pages 81-94

Depurination of A4256 in 28 S rRNA by the ribosome-inactivating proteins from barley and ricin results in different ribosome conformations

Author keywords

Ribosome structure; Ribosome inactivating proteins; rRNA structure, dynamics and translation

Indexed keywords

RIBOSOME PROTEIN; RIBOSOME RNA; RICIN; RNA 28S;

EID: 17544386277     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0303     Document Type: Article
Times cited : (15)

References (72)
  • 1
    • 0014202809 scopus 로고
    • Effect of spectinomycin on polypeptide synthesis in extracts of Escherichia coli
    • Anderson, P., Davies, J. & Davis, B. D. (1967). Effect of spectinomycin on polypeptide synthesis in extracts of Escherichia coli. J. Mol. Biol. 29, 203-215.
    • (1967) J. Mol. Biol. , vol.29 , pp. 203-215
    • Anderson, P.1    Davies, J.2    Davis, B.D.3
  • 2
    • 0011611787 scopus 로고
    • Isolation and characterization of inhibitors of animal cell-free protein synthesis from barley seeds
    • Asano, K., Svensson, B. & Poulsen, F. M. (1984). Isolation and characterization of inhibitors of animal cell-free protein synthesis from barley seeds. Carlsberg Res. Commun. 49, 619-626.
    • (1984) Carlsberg Res. Commun. , vol.49 , pp. 619-626
    • Asano, K.1    Svensson, B.2    Poulsen, F.M.3
  • 3
    • 0342664214 scopus 로고
    • Influence of a protein synthesis inhibitor from barley seeds upon different steps of animal cell-free protein synthesis
    • Asano, K., Svensson, B., Poulsen, F. M., Nygård, O. & Nilsson, L. (1986). Influence of a protein synthesis inhibitor from barley seeds upon different steps of animal cell-free protein synthesis. Carlsberg Res. Commun. 51, 75-81.
    • (1986) Carlsberg Res. Commun. , vol.51 , pp. 75-81
    • Asano, K.1    Svensson, B.2    Poulsen, F.M.3    Nygård, O.4    Nilsson, L.5
  • 5
    • 0025008960 scopus 로고
    • Ribosomal RNA and protein mutants resistant to spectinomycin
    • Bilgin, N., Richter, A. A., Ehrenberg, M. & Dahlberg, A. E. (1990). Ribosomal RNA and protein mutants resistant to spectinomycin. EMBO J. 9, 735-739.
    • (1990) EMBO J. , vol.9 , pp. 735-739
    • Bilgin, N.1    Richter, A.A.2    Ehrenberg, M.3    Dahlberg, A.E.4
  • 6
    • 0015507328 scopus 로고
    • A procedure for the isolation of mammalian messenger ribonucleic acid
    • Brawerman, G., Mendecki, J. & Lee, S. Y. (1972). A procedure for the isolation of mammalian messenger ribonucleic acid. Biochemistry, 11, 637-641.
    • (1972) Biochemistry , vol.11 , pp. 637-641
    • Brawerman, G.1    Mendecki, J.2    Lee, S.Y.3
  • 7
    • 0024589101 scopus 로고
    • Effect of α-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes
    • Brigotti, M., Rambelli, F., Zamboni, M., Montanaro, L. & Sperti, S. (1989). Effect of α-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes. Biochem. J. 257, 723-727.
    • (1989) Biochem. J. , vol.257 , pp. 723-727
    • Brigotti, M.1    Rambelli, F.2    Zamboni, M.3    Montanaro, L.4    Sperti, S.5
  • 8
    • 0028359389 scopus 로고
    • Spectinomycin interacts specifically with the residues G1064 and C1192 in 16 S rRNA, thereby potentially freezing this molecule into an inactive conformation
    • Brink, M. F., Brink, G., Verbeet, M. P. & de Boer, H. A. (1994). Spectinomycin interacts specifically with the residues G1064 and C1192 in 16 S rRNA, thereby potentially freezing this molecule into an inactive conformation. Nucl. Acids Res. 22, 325-331.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 325-331
    • Brink, M.F.1    Brink, G.2    Verbeet, M.P.3    De Boer, H.A.4
  • 9
    • 0020658387 scopus 로고
    • Protection of ribosomal RNA from kethoxal in polyribosomes: Implication of specific sites in ribosome function
    • Brow, D. A. & Noller, H. F. (1983). Protection of ribosomal RNA from kethoxal in polyribosomes: implication of specific sites in ribosome function. J. Mol. Biol. 163, 27-46.
    • (1983) J. Mol. Biol. , vol.163 , pp. 27-46
    • Brow, D.A.1    Noller, H.F.2
  • 10
    • 0029099379 scopus 로고
    • Regions of 23 S ribosomal RNA proximal to transfer RNA bound at the P and E sites
    • Bullard, J. M., van Waes, M. A., Bucklin, D. J. & Hill, W. E. (1995). Regions of 23 S ribosomal RNA proximal to transfer RNA bound at the P and E sites. J. Mol. Biol. 252, 572-582.
    • (1995) J. Mol. Biol. , vol.252 , pp. 572-582
    • Bullard, J.M.1    Van Waes, M.A.2    Bucklin, D.J.3    Hill, W.E.4
  • 11
    • 0021733607 scopus 로고
    • Differences in physical and biological properties of 50 S ribosomes and 23 S RNAs derived from tight and loose couple 70 S ribosomes
    • Burma, D. P., Srivastava, A. K., Srivastava, S., Tewari, D. S., Dash, D. & Sengupta, S. K. (1984). Differences in physical and biological properties of 50 S ribosomes and 23 S RNAs derived from tight and loose couple 70 S ribosomes. Biochem. Biophys. Res. Commun. 124, 970-978.
    • (1984) Biochem. Biophys. Res. Commun. , vol.124 , pp. 970-978
    • Burma, D.P.1    Srivastava, A.K.2    Srivastava, S.3    Tewari, D.S.4    Dash, D.5    Sengupta, S.K.6
  • 12
    • 78651145301 scopus 로고
    • Characterization of a ribosome-linked guanosine triphosphatase in Escherichia coli extracts
    • Conway, T. W. & Lipman, F. (1964). Characterization of a ribosome-linked guanosine triphosphatase in Escherichia coli extracts. Proc. Natl Acad. Sci. USA, 52, 1462-1469.
    • (1964) Proc. Natl Acad. Sci. USA , vol.52 , pp. 1462-1469
    • Conway, T.W.1    Lipman, F.2
  • 13
    • 0002241318 scopus 로고
    • Involvement of specific portions of ribosomal RNA in defined ribosomal functions: A study utilizing antibiotics
    • Hardesty B. & Kramer, G., eds, Springer, New York
    • Cundliffe, E. (1986). Involvement of specific portions of ribosomal RNA in defined ribosomal functions: a study utilizing antibiotics. In Structure, Function and Genetics of Ribosomes (Hardesty B. & Kramer, G., eds), pp. 586-604. Springer, New York.
    • (1986) Structure, Function and Genetics of Ribosomes , pp. 586-604
    • Cundliffe, E.1
  • 14
    • 0017074438 scopus 로고
    • Role of 5 S RNA in assembly and function of the 50 S subunit from Escherichia coli
    • Dohme, F. & Nierhaus, K. N. (1976). Role of 5 S RNA in assembly and function of the 50 S subunit from Escherichia coli. Proc. Natl Acad. Sci. USA, 73, 2221-2225.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2221-2225
    • Dohme, F.1    Nierhaus, K.N.2
  • 16
    • 0026601409 scopus 로고
    • Functional interactions within 23 S rRNA involving the peptidyl transferase centre
    • Douthwaite, S. (1992). Functional interactions within 23 S rRNA involving the peptidyl transferase centre. J. Bacteriol. 174, 1333-1338.
    • (1992) J. Bacteriol. , vol.174 , pp. 1333-1338
    • Douthwaite, S.1
  • 17
    • 0022330611 scopus 로고
    • Evidence for functional interaction between domains II and V of 23 S ribosomal RNA from an erythromycin resistant mutant
    • Douthwaite, S., Prince, J. B. & Noller, H. F. (1985). Evidence for functional interaction between domains II and V of 23 S ribosomal RNA from an erythromycin resistant mutant. Proc. Natl Acad. Sci. USA, 82, 8330-8334.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 8330-8334
    • Douthwaite, S.1    Prince, J.B.2    Noller, H.F.3
  • 18
    • 0024388825 scopus 로고
    • Defining the structural requirements for a helix in 23 S ribosomal RNA that confers erythromycin resistance
    • Douthwaite, S., Powers, T., Lee, J. Y. & Noller, H. F. (1989). Defining the structural requirements for a helix in 23 S ribosomal RNA that confers erythromycin resistance. J. Mol. Biol. 209, 655-665.
    • (1989) J. Mol. Biol. , vol.209 , pp. 655-665
    • Douthwaite, S.1    Powers, T.2    Lee, J.Y.3    Noller, H.F.4
  • 19
    • 0024349978 scopus 로고
    • Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23 S rRNA
    • Egebjerg, J., Douthwaite, S. & Garrett, R. A. (1989). Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23 S rRNA. EMBO J. 8, 607-611.
    • (1989) EMBO J. , vol.8 , pp. 607-611
    • Egebjerg, J.1    Douthwaite, S.2    Garrett, R.A.3
  • 20
    • 0020479406 scopus 로고
    • The site of action of α-sarcin on eukaryotic ribosomes
    • Endo, Y. & Wool, I. G. (1982). The site of action of α-sarcin on eukaryotic ribosomes. J. Biol. Chem. 257, 9054-9060.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9054-9060
    • Endo, Y.1    Wool, I.G.2
  • 21
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins to ribosomes
    • Endo, Y., Motizuki, M. & Tsurugi, K. (1987). The mechanism of action of ricin and related toxic lectins to ribosomes. J. Biol. Chem. 262, 5908-5912.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5908-5912
    • Endo, Y.1    Motizuki, M.2    Tsurugi, K.3
  • 22
    • 0024291090 scopus 로고
    • The mechanism of action of barley toxin: A type I ribosome-inactivating protein with RNA N-glycosidase activity
    • Endo, Y., Tsurugi, K. & Ebert, R. F. (1988). The mechanism of action of barley toxin: a type I ribosome-inactivating protein with RNA N-glycosidase activity. Biochim. Biophys. Acta, 954, 224-226.
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 224-226
    • Endo, Y.1    Tsurugi, K.2    Ebert, R.F.3
  • 23
    • 0017405550 scopus 로고
    • Effects of some proteins that inactivate the eukaryotic ribosome
    • Fernandez-Puentes, C. & Vazquez, D. (1977). Effects of some proteins that inactivate the eukaryotic ribosome. FEBS Letters, 78, 143-146.
    • (1977) FEBS Letters , vol.78 , pp. 143-146
    • Fernandez-Puentes, C.1    Vazquez, D.2
  • 24
    • 0028071557 scopus 로고
    • Collection of small subunit (16 S- and 16 S-like) ribosomal RNA structures: 1994
    • Gutell, R. R. (1994). Collection of small subunit (16 S- and 16 S-like) ribosomal RNA structures: 1994. Nucl. Acids Res. 22, 3502-3507.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3502-3507
    • Gutell, R.R.1
  • 25
    • 0027225783 scopus 로고
    • A compilation of large subuit (23 S and 23 S-like) ribosomal RNA structures Nucl
    • Gutell, R. R., Gray, M. W. & Schnare, M. N. (1993). A compilation of large subuit (23 S and 23 S-like) ribosomal RNA structures Nucl. Acids Res. 21, 3055-3074.
    • (1993) Acids Res. , vol.21 , pp. 3055-3074
    • Gutell, R.R.1    Gray, M.W.2    Schnare, M.N.3
  • 26
    • 0028261409 scopus 로고
    • Lessons from an evolving rRNA: 16 and 23 S rRNA structures from a comparative perspective
    • Gutell, R. R., Larsen, N. & Woese, C. R. (1994). Lessons from an evolving rRNA: 16 and 23 S rRNA structures from a comparative perspective. Microbiol. Rev. 58, 10-26.
    • (1994) Microbiol. Rev. , vol.58 , pp. 10-26
    • Gutell, R.R.1    Larsen, N.2    Woese, C.R.3
  • 27
    • 0023821349 scopus 로고
    • 3H]-p-azidopuromycin photoaffinity labeling of Escherichia coli ribosomes: Evidence for site-specific interaction at U-2504 and G-2502 in domain V of 23 S ribosomal RNA
    • 3H]-p-azidopuromycin photoaffinity labeling of Escherichia coli ribosomes: evidence for site-specific interaction at U-2504 and G-2502 in domain V of 23 S ribosomal RNA. Biochemistry, 27, 3983-3990.
    • (1988) Biochemistry , vol.27 , pp. 3983-3990
    • Hall, C.C.1    Johnson, D.2    Cooperman, B.S.3
  • 28
    • 0017159814 scopus 로고
    • Structural dynamics of bacterial ribosomes
    • Hapke & Noll. (1976). Structural dynamics of bacterial ribosomes. J. Mol. Biol. 105, 97-109.
    • (1976) J. Mol. Biol. , vol.105 , pp. 97-109
    • Hapke1    Noll2
  • 29
    • 0023405923 scopus 로고
    • Evidence that the G2261 region of 23 S rRNA is located at the ribosomal binding site of both elongation factors
    • Hausner, T. P., Atmadja, J. & Nierhaus, K. (1987). Evidence that the G2261 region of 23 S rRNA is located at the ribosomal binding site of both elongation factors. Biochimie, 69, 911-923.
    • (1987) Biochimie , vol.69 , pp. 911-923
    • Hausner, T.P.1    Atmadja, J.2    Nierhaus, K.3
  • 30
    • 0028609495 scopus 로고
    • Interaction sites of ribosome bound eukaryotic elongation factor 2 in 18 S and 28 S rRNA
    • Holmberg, L. & Nygård, O. (1994). Interaction sites of ribosome bound eukaryotic elongation factor 2 in 18 S and 28 S rRNA. Biochemistry, 33, 15159-15167.
    • (1994) Biochemistry , vol.33 , pp. 15159-15167
    • Holmberg, L.1    Nygård, O.2
  • 31
    • 0026800847 scopus 로고
    • Ribosome-bound eukaryotic elongation factor 2 protects 5 S rRNA from modification
    • Holmberg, L., Melander, Y. & Nygård, O. (1992). Ribosome-bound eukaryotic elongation factor 2 protects 5 S rRNA from modification. J. Biol. Chem. 267, 21906-21910.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21906-21910
    • Holmberg, L.1    Melander, Y.2    Nygård, O.3
  • 32
    • 0028102043 scopus 로고
    • Probing the conformational changes in 5.8 S, 18 S and 28 S rRNA upon association of derived subunits into complete 80 S ribosomes
    • Holmberg, L., Melander, Y. & Nygård, O. (1994a). Probing the conformational changes in 5.8 S, 18 S and 28 S rRNA upon association of derived subunits into complete 80 S ribosomes. Nucl. Acids Res. 22, 2776-2783.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 2776-2783
    • Holmberg, L.1    Melander, Y.2    Nygård, O.3
  • 33
    • 0028308319 scopus 로고
    • Probing the structure of mouse Ehrlich ascites cell 5.8 S, 18 S and 28 S ribosomal RNA in situ
    • Holmberg, L., Melander, Y. & Nygård, O. (1994b). Probing the structure of mouse Ehrlich ascites cell 5.8 S, 18 S and 28 S ribosomal RNA in situ. Nucl. Acids Res. 22, 1374-1382.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 1374-1382
    • Holmberg, L.1    Melander, Y.2    Nygård, O.3
  • 34
    • 0028944493 scopus 로고
    • A new mutation in 16 S rRNA of E. Coli conferring spectinomycin resistance
    • Johanson, U. & Hughes, D. (1995). A new mutation in 16 S rRNA of E. coli conferring spectinomycin resistance. Nucl. Acids Res. 23, 464-466.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 464-466
    • Johanson, U.1    Hughes, D.2
  • 35
    • 0028269333 scopus 로고
    • A conserved secondary structural motif in 23 S rRNA defines the site of interaction of amicetin, a universal inhibitor of peptide bond formation
    • Leviev, I. G., Rodriguez-Fonseca, C., Phan, H., Garrett, R. A., Heilek, G., Noller, H. F. &, Mankin, A. S. (1994). A conserved secondary structural motif in 23 S rRNA defines the site of interaction of amicetin, a universal inhibitor of peptide bond formation. EMBO J. 13, 1682-1686.
    • (1994) EMBO J. , vol.13 , pp. 1682-1686
    • Leviev, I.G.1    Rodriguez-Fonseca, C.2    Phan, H.3    Garrett, R.A.4    Heilek, G.5    Noller, H.F.6    Mankin, A.S.7
  • 37
    • 0023604801 scopus 로고
    • Spectinomycin resistance at site 1192 in 16 S ribosomal RNA of E. Coli: An analysis of three mutants
    • Makosky P. C. & Dahlberg, A. E. (1987). Spectinomycin resistance at site 1192 in 16 S 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
  • 38
    • 0025140986 scopus 로고
    • Selective cleavage and detailed analysis of intra-RNA cross-links induced in the large ribosomal subunit of E. Coli: A model for the tertiary structure of the tRNA binding domain in 23 S RNA
    • Mitchell, P., Osswald, M., Schueler, D. & Brimacombe, R. (1990). Selective cleavage and detailed analysis of intra-RNA cross-links induced in the large ribosomal subunit of E. coli: a model for the tertiary structure of the tRNA binding domain in 23 S RNA. Nucl. Acids Res. 18, 4325-4333.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 4325-4333
    • Mitchell, P.1    Osswald, M.2    Schueler, D.3    Brimacombe, R.4
  • 39
    • 0023604799 scopus 로고
    • Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23 S ribosomal RNA
    • Moazed, D. & Noller, H. F. (1987a). Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23 S ribosomal RNA. Biochimie, 69, 879-884.
    • (1987) Biochimie , vol.69 , pp. 879-884
    • Moazed, D.1    Noller, H.F.2
  • 40
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16 S ribosomal RNA
    • Moazed, D. & Noller, H. F. (1987b). Interaction of antibiotics with functional sites in 16 S ribosomal RNA. Nature, 327, 389-394.
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 41
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23 S rRNA in the ribosomal A, P, and E sites
    • Moazed, D. & Noller, H. F. (1989). Interaction of tRNA with 23 S 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
  • 42
    • 0023722010 scopus 로고
    • Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23 S RNA
    • Moazed, D., Robertson, J. M. & Noller, H. F. (1988). Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23 S RNA. Nature, 334, 362-364.
    • (1988) Nature , vol.334 , pp. 362-364
    • Moazed, D.1    Robertson, J.M.2    Noller, H.F.3
  • 43
    • 0014219466 scopus 로고
    • Catalysis of peptide bond formation by 50 S ribosomal subunits from Escherichia coli
    • Monro, R. E. (1967). Catalysis of peptide bond formation by 50 S ribosomal subunits from Escherichia coli. J. Mol. Biol. 26, 147-151.
    • (1967) J. Mol. Biol. , vol.26 , pp. 147-151
    • Monro, R.E.1
  • 44
    • 0015801982 scopus 로고
    • Inhibition by ricin of protein synthesis in vitro: Ribosomes as the target of the toxin
    • Montanaro, L., Sperti, S. & Stirpe, F. (1973). Inhibition by ricin of protein synthesis in vitro: ribosomes as the target of the toxin. Biochem. J. 136, 677-683.
    • (1973) Biochem. J. , vol.136 , pp. 677-683
    • Montanaro, L.1    Sperti, S.2    Stirpe, F.3
  • 45
    • 0022881369 scopus 로고
    • The mechanism of the protein-synthesis elongation cycle in eukaryotes: Effect of ricin on the ribosomal interaction with elongation factors
    • Nilsson, L. & Nygård, O. (1986). The mechanism of the protein-synthesis elongation cycle in eukaryotes: effect of ricin on the ribosomal interaction with elongation factors. Eur. J. Biochem. 161, 111-117.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 111-117
    • Nilsson, L.1    Nygård, O.2
  • 46
    • 0022529307 scopus 로고
    • Reduced turnover of the elongation factor EF-1-ribosome complex after treatment with the protein synthesis inhibitor (II) from barley seeds
    • Nilsson, L., Asano, K., Svensson, B., Poulsen, F. M. & Nygård, O. (1986). Reduced turnover of the elongation factor EF-1-ribosome complex after treatment with the protein synthesis inhibitor (II) from barley seeds. Biochim. Biophys. Acta, 868, 62-70.
    • (1986) Biochim. Biophys. Acta , vol.868 , pp. 62-70
    • Nilsson, L.1    Asano, K.2    Svensson, B.3    Poulsen, F.M.4    Nygård, O.5
  • 47
    • 0025733603 scopus 로고
    • Ribosomal RNA and translation
    • Noller, H. F. (1991). Ribosomal RNA and translation. Annu. Rev. Biochem. 60, 191-227.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 191-227
    • Noller, H.F.1
  • 48
    • 0020337793 scopus 로고
    • Identification by RNA-protein cross-linking of ribosomal proteins located at the interface between the small and the large subunits of mammalian ribosomes
    • Nygård, O. & Nika, H. (1982). Identification by RNA-protein cross-linking of ribosomal proteins located at the interface between the small and the large subunits of mammalian ribosomes. EMBO J. 1, 357-362.
    • (1982) EMBO J. , vol.1 , pp. 357-362
    • Nygård, O.1    Nika, H.2
  • 49
    • 0024514137 scopus 로고
    • Characterization of the ribosomal properties required for formation of a GTPase active complex with the eukaryotic elongation factor 2
    • Nygård, O. & Nilsson, L. (1989). Characterization of the ribosomal properties required for formation of a GTPase active complex with the eukaryotic elongation factor 2. Eur. J. Biochem. 179, 603-608.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 603-608
    • Nygård, O.1    Nilsson, L.2
  • 50
    • 0025291205 scopus 로고
    • Translational dynamics: Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis
    • Nygård, O. & Nilsson, L. (1990). Translational dynamics: interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis. Eur. J. Biochem. 191, 1-17.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 1-17
    • Nygård, O.1    Nilsson, L.2
  • 51
    • 0029617892 scopus 로고
    • The involvement of two distinct regions of 23 S ribosomal RNA in tRNA selection
    • O'Connor, M. & Dahlberg, A. E. (1995). The involvement of two distinct regions of 23 S ribosomal RNA in tRNA selection. J. Mol. Biol. 254, 838-847.
    • (1995) J. Mol. Biol. , vol.254 , pp. 838-847
    • O'Connor, M.1    Dahlberg, A.E.2
  • 52
    • 0015781481 scopus 로고
    • Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis
    • Olsnes, S. & Pihl, A. (1973). Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis. Biochemistry, 12, 3121-3126.
    • (1973) Biochemistry , vol.12 , pp. 3121-3126
    • Olsnes, S.1    Pihl, A.2
  • 53
    • 0029011424 scopus 로고
    • Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenisis approach
    • Porse, B. T. & Garrett, R. A. (1995). Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenisis approach. J. Mol. Biol. 249, 1-10.
    • (1995) J. Mol. Biol. , vol.249 , pp. 1-10
    • Porse, B.T.1    Garrett, R.A.2
  • 55
    • 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., Amils, R. & Garrett, R. A. (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    Amils, R.2    Garrett, R.A.3
  • 56
    • 0027732617 scopus 로고
    • 4 and the antibiotic thiostrepton interact with overlapping regions of the 23 S rRNA backbone in the ribosomal GTPase centre
    • 4 and the 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    Douthwaite, S.2
  • 57
    • 0025931608 scopus 로고
    • Evidence for a competitive-displacement model for the initiation of protein synthesis involving intermolecular hybridization of 5 S rRNA, 18 S rRNA and mRNA
    • Sarge, K. D. & Maxwell, E. S. (1991). Evidence for a competitive-displacement model for the initiation of protein synthesis involving intermolecular hybridization of 5 S rRNA, 18 S rRNA and mRNA. FEBS Letters, 294, 234-238.
    • (1991) FEBS Letters , vol.294 , pp. 234-238
    • Sarge, K.D.1    Maxwell, E.S.2
  • 58
    • 0021760461 scopus 로고
    • Antibiotic resistance mutations in 16 S and 23 S ribosomal RNA genes of Escherichia coli
    • Sigmund, C. D., Ettayebi, M. & Morgan, E. A. (1984). Antibiotic resistance mutations in 16 S and 23 S ribosomal RNA genes of Escherichia coli. Nucl. Acids Res. 12, 4653-4663.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 4653-4663
    • Sigmund, C.D.1    Ettayebi, M.2    Morgan, E.A.3
  • 59
    • 0021112383 scopus 로고
    • Chemical crosslinking of elongation factor G to the 23 S RNA in 70 S ribosomes from Escherichia coli
    • Sköld, S.-E. (1983). Chemical crosslinking of elongation factor G to the 23 S RNA in 70 S ribosomes from Escherichia coli. Nucl. Acids Res. 11, 4923-4932.
    • (1983) Nucl. Acids Res. , vol.11 , pp. 4923-4932
    • Sköld, S.-E.1
  • 60
    • 0014636203 scopus 로고
    • A model of the functioning ribosome: Locking and unlocking of the ribosome subparticles
    • Spirin, A. S. (1967). A model of the functioning ribosome: locking and unlocking of the ribosome subparticles. Cold Spring Harbor Symp. Quant. Biol. 14, 197-207.
    • (1967) Cold Spring Harbor Symp. Quant. Biol. , vol.14 , pp. 197-207
    • Spirin, A.S.1
  • 62
    • 0029055199 scopus 로고
    • Mapping the path of the nascent peptide chain through the 23 S RNA in the 50 S ribosomal subunit
    • Stade, K., Junke, N. & Brimacombe, R. (1995). Mapping the path of the nascent peptide chain through the 23 S RNA in the 50 S ribosomal subunit. Nucl. Acids Res. 23, 2371-2380.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2371-2380
    • Stade, K.1    Junke, N.2    Brimacombe, R.3
  • 63
    • 0024227741 scopus 로고
    • Photo-affinity labelling at the peptidyl transferase centre reveals two different positions for the A- and P-sites in domain V of 23 S rRNA
    • Steiner, G., Kuechler, E. & Barta, A. (1988). Photo-affinity labelling at the peptidyl transferase centre reveals two different positions for the A- and P-sites in domain V of 23 S rRNA. EMBO J. 7, 3949-3955.
    • (1988) EMBO J. , vol.7 , pp. 3949-3955
    • Steiner, G.1    Kuechler, E.2    Barta, A.3
  • 64
    • 0016622605 scopus 로고
    • Structure and function of free 40 S ribosome subunits: Characterization of initiation factors
    • Sundkvist, I. C. & Staehelin, T. (1975). Structure and function of free 40 S ribosome subunits: characterization of initiation factors. J. Mol. Biol. 99, 401-418.
    • (1975) J. Mol. Biol. , vol.99 , pp. 401-418
    • Sundkvist, I.C.1    Staehelin, T.2
  • 65
    • 0028953727 scopus 로고
    • The α-sarcin/ricin loop, a modular RNA
    • Szewczak, A. A. & Moore, P. B. (1995). The α-sarcin/ricin loop, a modular RNA. J. Mol. Biol. 247, 81-98.
    • (1995) J. Mol. Biol. , vol.247 , pp. 81-98
    • Szewczak, A.A.1    Moore, P.B.2
  • 66
    • 0027484279 scopus 로고
    • The conformation of the α-sarcin/ricin loop from 28 S ribosomal RNA
    • Szewczak, A. A., Moore, P. B., Chan, Y.-L. & Wool, I. G. (1993). The conformation of the α-sarcin/ricin loop from 28 S ribosomal RNA. Proc. Natl Acad. Sci. USA, 90, 9581-9585.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9581-9585
    • Szewczak, A.A.1    Moore, P.B.2    Chan, Y.-L.3    Wool, I.G.4
  • 67
    • 0028446541 scopus 로고
    • Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection
    • Taylor, S., Massiah, A., Lomonossoff, G., Roberts, L. M., Lord, J. M. & Hartley, M. (1994). Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection. Plant J. 5, 827-835.
    • (1994) Plant J. , vol.5 , pp. 827-835
    • Taylor, S.1    Massiah, A.2    Lomonossoff, G.3    Roberts, L.M.4    Lord, J.M.5    Hartley, M.6
  • 68
    • 0024287862 scopus 로고
    • Ricin and α-sarcin alter the conformation of 60 S ribosomal subunits at neighboring but different sites
    • Terao, K. T., Uchiumi, T., Endo, Y. & Ogata, K. (1988). Ricin and α-sarcin alter the conformation of 60 S ribosomal subunits at neighboring but different sites. Eur. J. Biochem. 174, 459-463.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 459-463
    • Terao, K.T.1    Uchiumi, T.2    Endo, Y.3    Ogata, K.4
  • 69
    • 0015750298 scopus 로고
    • The association of ribosomal subunits of Escherichia coli. 1. Two types of association products differing in their apparent sedimentation coefficient
    • van Diggelen, O. P. & Bosch, L. (1973). The association of ribosomal subunits of Escherichia coli. 1. Two types of association products differing in their apparent sedimentation coefficient. Eur. J. Biochem. 39, 499-510.
    • (1973) Eur. J. Biochem. , vol.39 , pp. 499-510
    • Diggelen, O.P.1    Bosch, L.2
  • 70
    • 0015731564 scopus 로고
    • The association of ribosomal subunits of Escherichia coli. 2. Two types of association products differing in sensitivity to hydrostatic pressure generated during centrifugation
    • van Diggelen, O. P., Oostrom, H. & Bosch, L. (1973). The association of ribosomal subunits of Escherichia coli. 2. Two types of association products differing in sensitivity to hydrostatic pressure generated during centrifugation. Eur. J. Biochem. 39, 511-523.
    • (1973) Eur. J. Biochem. , vol.39 , pp. 511-523
    • Van Diggelen, O.P.1    Oostrom, H.2    Bosch, L.3
  • 71
    • 0026690643 scopus 로고
    • Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation
    • Wool, I. G., Gluck, 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    Gluck, A.2    Endo, Y.3
  • 72
    • 0025019258 scopus 로고
    • 500-MHz proton evidence for two solution structures of the common arm base-paired segment of wheat germ 5 S ribosomal RNA
    • Wu, J. & Marshall, A. G. (1990). 500-MHz proton evidence for two solution structures of the common arm base-paired segment of wheat germ 5 S ribosomal RNA. Biochemistry, 29, 1722-1730.
    • (1990) Biochemistry , vol.29 , pp. 1722-1730
    • Wu, J.1    Marshall, A.G.2


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