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Volumn 10, Issue 8, 2003, Pages 769-778

Structural basis for contrasting activities of ribosome binding thiazole antibiotics

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EID: 0042415065     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(03)00173-X     Document Type: Article
Times cited : (84)

References (48)
  • 2
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289:2000;905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 6
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan V. Ribosome structure and the mechanism of translation. Cell. 108:2002;557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 7
    • 0019810825 scopus 로고
    • The binding site for ribosomal protein L11 within 23 S ribosomal RNA of Escherichia coli
    • Schmidt F.J., Thompson J., Lee K., Dijk J., Cundliffe E. The binding site for ribosomal protein L11 within 23 S ribosomal RNA of Escherichia coli. J. Biol. Chem. 256:1981;12301-12305.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12301-12305
    • Schmidt, F.J.1    Thompson, J.2    Lee, K.3    Dijk, J.4    Cundliffe, E.5
  • 8
    • 0025330496 scopus 로고
    • Characterization of the binding sites of protein L11 and the L10.(L12)4 pentameric complex in the GTPase domain of 23 S ribosomal RNA from Escherichia coli
    • Egebjerg J., Douthwaite S.R., Liljas A., Garrett R.A. Characterization of the binding sites of protein L11 and the L10.(L12)4 pentameric complex in the GTPase domain of 23 S ribosomal RNA from Escherichia coli. J. Mol. Biol. 213:1990;275-288.
    • (1990) J. Mol. Biol. , vol.213 , pp. 275-288
    • Egebjerg, J.1    Douthwaite, S.R.2    Liljas, A.3    Garrett, R.A.4
  • 9
    • 0021112383 scopus 로고
    • Chemical crosslinking of elongation factor G to the 23S RNA in 70S ribosomes from Escherichia coli
    • Sköld S.E. Chemical crosslinking of elongation factor G to the 23S RNA in 70S ribosomes from Escherichia coli. Nucleic Acids Res. 11:1983;4923-4932.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 4923-4932
    • Sköld, S.E.1
  • 10
    • 0023722010 scopus 로고
    • Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA
    • Moazed D., Robertson J.M., Noller H.F. Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA. Nature. 334:1988;362-364.
    • (1988) Nature , vol.334 , pp. 362-364
    • Moazed, D.1    Robertson, J.M.2    Noller, H.F.3
  • 11
    • 0034456004 scopus 로고    scopus 로고
    • Translational elongation factor G: A GTP-driven motor of the ribosome
    • Wintermeyer W., Rodnina M.V. Translational elongation factor G. a GTP-driven motor of the ribosome Essays Biochem. 35:2000;117-129.
    • (2000) Essays Biochem. , vol.35 , pp. 117-129
    • Wintermeyer, W.1    Rodnina, M.V.2
  • 13
    • 0020419248 scopus 로고
    • Site of action of a ribosomal RNA methyltransferase conferring resistance to thiostrepton
    • Thompson J., Schmidt F., Cundliffe E. Site of action of a ribosomal RNA methyltransferase conferring resistance to thiostrepton. J. Biol. Chem. 257:1982;7915-7917.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7915-7917
    • Thompson, J.1    Schmidt, F.2    Cundliffe, E.3
  • 15
    • 0036301166 scopus 로고    scopus 로고
    • Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome
    • Cameron D.M., Thompson J., March P.E., Dahlberg A.E. Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome. J. Mol. Biol. 319:2002;27-35.
    • (2002) J. Mol. Biol. , vol.319 , pp. 27-35
    • Cameron, D.M.1    Thompson, J.2    March, P.E.3    Dahlberg, A.E.4
  • 16
    • 0028355760 scopus 로고
    • The antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A
    • Rosendahl G., Douthwaite S. The antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A. Nucleic Acids Res. 22:1994;357-363.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 357-363
    • Rosendahl, G.1    Douthwaite, S.2
  • 17
    • 0024349978 scopus 로고
    • Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23S rRNA
    • Egebjerg J., Douthwaite S., Garrett R.A. Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23S rRNA. EMBO J. 8:1989;607-611.
    • (1989) EMBO J. , vol.8 , pp. 607-611
    • Egebjerg, J.1    Douthwaite, S.2    Garrett, R.A.3
  • 18
    • 0032548821 scopus 로고    scopus 로고
    • The antibiotic thiostrepton inhibits a functional transition within protein L11 at the ribosomal GTPase centre
    • Porse B.T., Leviev I., Mankin A.S., Garrett R.A. The antibiotic thiostrepton inhibits a functional transition within protein L11 at the ribosomal GTPase centre. J. Mol. Biol. 276:1998;391-404.
    • (1998) J. Mol. Biol. , vol.276 , pp. 391-404
    • Porse, B.T.1    Leviev, I.2    Mankin, A.S.3    Garrett, R.A.4
  • 19
    • 0030020855 scopus 로고    scopus 로고
    • Cooperative interactions of RNA and thiostrepton antibiotic with two domains of ribosomal protein L11
    • Xing Y., Draper D.E. Cooperative interactions of RNA and thiostrepton antibiotic with two domains of ribosomal protein L11. Biochemistry. 35:1996;1581-1588.
    • (1996) Biochemistry , vol.35 , pp. 1581-1588
    • Xing, Y.1    Draper, D.E.2
  • 20
    • 0018351356 scopus 로고
    • Ribose methylation and resistance to thiostrepton
    • Cundliffe E., Thompson J. Ribose methylation and resistance to thiostrepton. Nature. 278:1979;859-861.
    • (1979) Nature , vol.278 , pp. 859-861
    • Cundliffe, E.1    Thompson, J.2
  • 21
    • 0021753590 scopus 로고
    • Identification of the altered ribosomal component responsible for resistance to micrococcin in mutants of Bacillus megaterium
    • Spedding G., Cundliffe E. Identification of the altered ribosomal component responsible for resistance to micrococcin in mutants of Bacillus megaterium. Eur. J. Biochem. 140:1984;453-459.
    • (1984) Eur. J. Biochem. , vol.140 , pp. 453-459
    • Spedding, G.1    Cundliffe, E.2
  • 22
    • 0019483431 scopus 로고
    • Concerning the mode of action of micrococcin upon bacterial protein synthesis
    • Cundliffe E., Thompson J. Concerning the mode of action of micrococcin upon bacterial protein synthesis. Eur. J. Biochem. 118:1981;47-52.
    • (1981) Eur. J. Biochem. , vol.118 , pp. 47-52
    • Cundliffe, E.1    Thompson, J.2
  • 23
    • 0026005654 scopus 로고
    • The binding of thiostrepton to 23S ribosomal RNA
    • Thompson J., Cundliffe E. The binding of thiostrepton to 23S ribosomal RNA. Biochimie. 73:1991;1131-1135.
    • (1991) Biochimie , vol.73 , pp. 1131-1135
    • Thompson, J.1    Cundliffe, E.2
  • 24
    • 0033553439 scopus 로고    scopus 로고
    • A detailed view of a ribosomal active site: The structure of the L11-RNA complex
    • Wimberly B.T., Guymon R., McCutcheon J.P., White S.W., Ramakrishnan V. A detailed view of a ribosomal active site. the structure of the L11-RNA complex Cell. 4:1999;491-502.
    • (1999) Cell , vol.4 , pp. 491-502
    • Wimberly, B.T.1    Guymon, R.2    McCutcheon, J.P.3    White, S.W.4    Ramakrishnan, V.5
  • 25
    • 0033553625 scopus 로고    scopus 로고
    • Crystal structure of a conserved ribosomal protein-RNA complex
    • Conn G.L., Draper D.E., Lattman E.E., Gittis A.G. Crystal structure of a conserved ribosomal protein-RNA complex. Science. 284:1999;1171-1174.
    • (1999) Science , vol.284 , pp. 1171-1174
    • Conn, G.L.1    Draper, D.E.2    Lattman, E.E.3    Gittis, A.G.4
  • 26
    • 0027933451 scopus 로고
    • Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2′-methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA
    • Bechthold A., Floss H.G. Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2′-methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA. Eur. J. Biochem. 224:1994;431-437.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 431-437
    • Bechthold, A.1    Floss, H.G.2
  • 27
    • 0025999688 scopus 로고
    • Recognition of the highly conserved GTPase center of 23 S ribosomal RNA by ribosomal protein L11 and the antibiotic thiostrepton
    • Ryan P.C., Lu M., Draper D.E. Recognition of the highly conserved GTPase center of 23 S ribosomal RNA by ribosomal protein L11 and the antibiotic thiostrepton. J. Mol. Biol. 221:1991;1257-1268.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1257-1268
    • Ryan, P.C.1    Lu, M.2    Draper, D.E.3
  • 29
    • 0035024041 scopus 로고    scopus 로고
    • Structure of the macrocycle thiostrepton solved using the anomalous dispersion contribution of sulfur
    • Bond C.S., Shaw M.P., Alphey M.S., Hunter W.N. Structure of the macrocycle thiostrepton solved using the anomalous dispersion contribution of sulfur. Acta Crystallogr. D Biol. Crystallogr. 57:2001;755-758.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 755-758
    • Bond, C.S.1    Shaw, M.P.2    Alphey, M.S.3    Hunter, W.N.4
  • 31
    • 0034649618 scopus 로고    scopus 로고
    • Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations
    • Bissantz C., Folkers G., Rognan D. Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations. J. Med. Chem. 43:2000;4759-4767.
    • (2000) J. Med. Chem. , vol.43 , pp. 4759-4767
    • Bissantz, C.1    Folkers, G.2    Rognan, D.3
  • 32
    • 0014940646 scopus 로고
    • Studies on translocation. 3. Conditions necessary for the formation and detection of a stable ribosome-G factor-guanosine diphosphate complex in the presence of fusidic acid
    • Bodley J.W., Zieve F.J., Lin L., Zieve S.T. Studies on translocation. 3. Conditions necessary for the formation and detection of a stable ribosome-G factor-guanosine diphosphate complex in the presence of fusidic acid. J. Biol. Chem. 245:1970;5656-5661.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5656-5661
    • Bodley, J.W.1    Zieve, F.J.2    Lin, L.3    Zieve, S.T.4
  • 33
    • 0019857109 scopus 로고
    • The mode of action of nosiheptide (multhiomycin) and the mechanism of resistance in the producing organism
    • Cundliffe E., Thompson J. The mode of action of nosiheptide (multhiomycin) and the mechanism of resistance in the producing organism. J. Gen. Microbiol. 126:1981;185-192.
    • (1981) J. Gen. Microbiol. , vol.126 , pp. 185-192
    • Cundliffe, E.1    Thompson, J.2
  • 35
    • 0033583095 scopus 로고    scopus 로고
    • The antibiotic micrococcin acts on protein L11 at the ribosomal GTPase centre
    • Porse B.T., Cundliffe E., Garrett R.A. The antibiotic micrococcin acts on protein L11 at the ribosomal GTPase centre. J. Mol. Biol. 287:1999;33-45.
    • (1999) J. Mol. Biol. , vol.287 , pp. 33-45
    • Porse, B.T.1    Cundliffe, E.2    Garrett, R.A.3
  • 36
    • 0032498266 scopus 로고    scopus 로고
    • Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing
    • Wilson K.S., Noller H.F. Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing. Cell. 92:1998;131-139.
    • (1998) Cell , vol.92 , pp. 131-139
    • Wilson, K.S.1    Noller, H.F.2
  • 37
    • 0035943352 scopus 로고    scopus 로고
    • Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation
    • Agrawal R.K., Linde J., Sengupta J., Nierhaus K.H., Frank J. Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation. J. Mol. Biol. 311:2001;777-787.
    • (2001) J. Mol. Biol. , vol.311 , pp. 777-787
    • Agrawal, R.K.1    Linde, J.2    Sengupta, J.3    Nierhaus, K.H.4    Frank, J.5
  • 38
    • 0034603196 scopus 로고    scopus 로고
    • Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
    • Stark H., Rodnina M.V., Wieden H.J., van Heel M., Wintermeyer W. Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation. Cell. 100:2000;301-309.
    • (2000) Cell , vol.100 , pp. 301-309
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.J.3    Van Heel, M.4    Wintermeyer, W.5
  • 40
    • 0017963459 scopus 로고
    • Nature of the heterogeneity of 30S ribosomal subparticles in vitro. I. Effect of large centrifugal fields during 30S subparticle isolation on their capacity for codon-dependent tRNA binding
    • Kirillov S.V., Makhno V.I., Peshin N.N., Semenkov I.U. Nature of the heterogeneity of 30S ribosomal subparticles in vitro. I. Effect of large centrifugal fields during 30S subparticle isolation on their capacity for codon-dependent tRNA binding. Mol. Biol. (Mosk.). 12:1978;602-611.
    • (1978) Mol. Biol. (Mosk.) , vol.12 , pp. 602-611
    • Kirillov, S.V.1    Makhno, V.I.2    Peshin, N.N.3    Semenkov, I.U.4
  • 41
    • 0028941626 scopus 로고
    • GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs
    • Rodnina M., Wintermeyer W. GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs. Proc. Natl. Acad. Sci. USA. 92:1995;1945-1949.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1945-1949
    • Rodnina, M.1    Wintermeyer, W.2
  • 42
    • 0029994962 scopus 로고    scopus 로고
    • Truncated elongation factor G lacking the G domain promotes translocation of the 3′ end but not of the anticodon domain of peptidyl-tRNA
    • Borowski C., Rodnina M.V., Wintermeyer W. Truncated elongation factor G lacking the G domain promotes translocation of the 3′ end but not of the anticodon domain of peptidyl-tRNA. Proc. Natl. Acad. Sci. USA. 93:1996;4202-4206.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4202-4206
    • Borowski, C.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 43
    • 0034697995 scopus 로고    scopus 로고
    • Role of domains 4 and 5 in elongation factor G functions on the ribosome
    • Savelsbergh A., Matassova N., Rodnina M., Wintermeyer W. Role of domains 4 and 5 in elongation factor G functions on the ribosome. J. Mol. Biol. 300:2000;951-961.
    • (2000) J. Mol. Biol. , vol.300 , pp. 951-961
    • Savelsbergh, A.1    Matassova, N.2    Rodnina, M.3    Wintermeyer, W.4
  • 44
    • 0015871909 scopus 로고
    • In vitro synthesis of protein in microbial systems
    • Zubay G. In vitro synthesis of protein in microbial systems. Annu. Rev. Genet. 7:1973;267-287.
    • (1973) Annu. Rev. Genet. , vol.7 , pp. 267-287
    • Zubay, G.1
  • 46
    • 0002123344 scopus 로고    scopus 로고
    • Preparation of RNA:protein complexes for x-ray crystallography and NMR
    • C.W.J. Smith. Oxford: Oxford University Press. 37-74.pp
    • Price S.R., Oubridge C., Varani G., Nagai K. Preparation of RNA:protein complexes for x-ray crystallography and NMR. Smith C.W.J. RNA:Protein Interactions. 1998;Oxford University Press, Oxford. 37-74.pp.
    • (1998) RNA:Protein Interactions
    • Price, S.R.1    Oubridge, C.2    Varani, G.3    Nagai, K.4
  • 47
    • 0030571537 scopus 로고    scopus 로고
    • A novel plasmid vector that uses the glucose kinase gene (glkA) for the positive selection of stable gene disruptants in Streptomyces
    • van Wezel G.P., Bibb M.J. A novel plasmid vector that uses the glucose kinase gene (glkA) for the positive selection of stable gene disruptants in Streptomyces. Gene. 182:1996;229-230.
    • (1996) Gene , vol.182 , pp. 229-230
    • Van Wezel, G.P.1    Bibb, M.J.2


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