메뉴 건너뛰기




Volumn 41, Issue 5, 2001, Pages 1091-1099

The pleuromutilin drugs tiamulin and valnemulin bind to the RNA at the peptidyl transferase centre on the ribosome

Author keywords

[No Author keywords available]

Indexed keywords

CARBOMYCIN; ENZYME INHIBITOR; ERYTHROMYCIN; MACROLIDE; PEPTIDYLTRANSFERASE; PLEUROMUTILIN; RIBOSOME RNA; RNA; TIAMULIN; TRANSFER RNA; UNCLASSIFIED DRUG; VALNEMULIN;

EID: 0035788806     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2001.02595.x     Document Type: Article
Times cited : (168)

References (31)
  • 1
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P.B., and Steitz, T.A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289: 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
  • 2
    • 0032584065 scopus 로고    scopus 로고
    • 23S rRNA positions essential for tRNA binding in ribosomal functional sites
    • Bocchetta, M., Xiong, L., and Mankin, A.S. (1998) 23S rRNA positions essential for tRNA binding in ribosomal functional sites. Proc Natl Acad Sci USA 95: 3525-3530.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3525-3530
    • Bocchetta, M.1    Xiong, L.2    Mankin, A.S.3
  • 3
    • 0015230176 scopus 로고
    • Effects of macrolide antibiotics on the ribosomal peptidyl transferase in cell-free systems derived from Escherichia coli B and erythromycin-resistant mutant of Escherichia Coli B
    • Cerna, J., Jonak, J., and Rychlik, I. (1971) Effects of macrolide antibiotics on the ribosomal peptidyl transferase in cell-free systems derived from Escherichia coli B and erythromycin-resistant mutant of Escherichia Coli B. Biochim Biophys Acta 240: 109-121.
    • (1971) Biochim Biophys Acta , vol.240 , pp. 109-121
    • Cerna, J.1    Jonak, J.2    Rychlik, I.3
  • 4
    • 0018162344 scopus 로고
    • The effects of tiamulin, a semisynthetic pleuromutilin derivative, on bacterial polypeptide chain initiation
    • Dornhelm, P., and Högenauer, G. (1978) The effects of tiamulin, a semisynthetic pleuromutilin derivative, on bacterial polypeptide chain initiation. Eur J Biochem 91: 465-473.
    • (1978) Eur J Biochem , vol.91 , pp. 465-473
    • Dornhelm, P.1    Högenauer, G.2
  • 7
    • 0032972963 scopus 로고    scopus 로고
    • Reconstitution of functional 50S ribosomes from in vitro transcripts of Bacillus stearothermophilus 23S rRNA
    • Green, R., and Noller, H.F. (1999) Reconstitution of functional 50S ribosomes from in vitro transcripts of Bacillus stearothermophilus 23S rRNA. Biochemistry 38: 1772-1779.
    • (1999) Biochemistry , vol.38 , pp. 1772-1779
    • Green, R.1    Noller, H.F.2
  • 8
    • 0031566952 scopus 로고    scopus 로고
    • Mutations at nucleotides G2251 and U2585 of 23 S rRNA perturb the peptidyl transferase center of the ribosome
    • Green, R., Samaha, R.R., and Noller, H.F. (1997) Mutations at nucleotides G2251 and U2585 of 23 S rRNA perturb the peptidyl transferase center of the ribosome. J Mol Biol 266: 40-50.
    • (1997) J Mol Biol , vol.266 , pp. 40-50
    • Green, R.1    Samaha, R.R.2    Noller, H.F.3
  • 9
    • 0028261409 scopus 로고
    • Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective
    • Gutell, R.R., Larsen, N., and Woese, C.R. (1994) Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective. Microb Rev 58: 10-26.
    • (1994) Microb Rev , vol.58 , pp. 10-26
    • Gutell, R.R.1    Larsen, N.2    Woese, C.R.3
  • 10
    • 0016203943 scopus 로고
    • The mode of action of pleuromutilin derivatives. Effect on cell-free polypeptide synthesis
    • Hodgin, L.A., and Högenauer, G. (1974) The mode of action of pleuromutilin derivatives. Effect on cell-free polypeptide synthesis. Eur J Biochem 47: 527-533.
    • (1974) Eur J Biochem , vol.47 , pp. 527-533
    • Hodgin, L.A.1    Högenauer, G.2
  • 11
    • 0016668072 scopus 로고
    • The mode of action of pleuromutilin derivatives. Location and properties of the pleuromutilin binding site on Escherichia coli ribosomes
    • Högenauer, G. (1975) The mode of action of pleuromutilin derivatives. Location and properties of the pleuromutilin binding site on Escherichia coli ribosomes. Eur J Biochem 52: 93-98.
    • (1975) Eur J Biochem , vol.52 , pp. 93-98
    • Högenauer, G.1
  • 12
    • 0019435181 scopus 로고
    • Affinity labeling of Escherichia coli ribosomes with a covalently binding derivative of the antibiotic pleuromutilin
    • Högenauer, G., Egger, H., Ruf, C., and Stumper, B. (1981) Affinity labeling of Escherichia coli ribosomes with a covalently binding derivative of the antibiotic pleuromutilin. Biochemistry 20: 546-552.
    • (1981) Biochemistry , vol.20 , pp. 546-552
    • Högenauer, G.1    Egger, H.2    Ruf, C.3    Stumper, B.4
  • 13
    • 0001581071 scopus 로고
    • Antibiotic substances from basidomycetes. VIII. Pleurotus Multilus (Fr.) Sacc. & Pleurotus Passeckerianus Pilat
    • Kavanagh, F., Hervey, A., and Robbins, W.J. (1951) Antibiotic substances from basidomycetes. VIII. Pleurotus Multilus (Fr.) Sacc. & Pleurotus Passeckerianus Pilat. Proc Natl Acad Sci USA 37: 570-574.
    • (1951) Proc Natl Acad Sci USA , vol.37 , pp. 570-574
    • Kavanagh, F.1    Hervey, A.2    Robbins, W.J.3
  • 14
    • 0033231562 scopus 로고    scopus 로고
    • Base-pairing between 23S rRNA and tRNA in the ribosomal A site
    • Kim, D.F., and Green, R. (1999) Base-pairing between 23S rRNA and tRNA in the ribosomal A site. Mol Cell 4: 859-864.
    • (1999) Mol Cell , vol.4 , pp. 859-864
    • Kim, D.F.1    Green, R.2
  • 15
    • 0030904329 scopus 로고    scopus 로고
    • Movement of the 3′-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics
    • Kirillov, S., Porse, B.T., Vester, B., Woolley, P., and Garrett, R.A. (1997) Movement of the 3′-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics. FEBS Lett 406: 223-233.
    • (1997) FEBS Lett , vol.406 , pp. 223-233
    • Kirillov, S.1    Porse, B.T.2    Vester, B.3    Woolley, P.4    Garrett, R.A.5
  • 16
    • 0032818296 scopus 로고    scopus 로고
    • Peptidyl transferase antibiotics perturb the relative positioning of the 3′-terminal adenosine of P/P′-site-bound tRNA and 23S rRNA in the ribosome
    • Kirillov, S.V., Porse, B.T., and Garrett, R.A. (1999) Peptidyl transferase antibiotics perturb the relative positioning of the 3′-terminal adenosine of P/P′-site-bound tRNA and 23S rRNA in the ribosome. RNA 5: 1003-1013.
    • (1999) RNA , vol.5 , pp. 1003-1013
    • Kirillov, S.V.1    Porse, B.T.2    Garrett, R.A.3
  • 17
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites
    • Moazed, D., and Noller, H.F. (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
  • 18
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen, P., Hansen, J., Ban, N., Moore, P.B., and Steitz, T.A. (2000) The structural basis of ribosome activity in peptide bond synthesis. Science 289: 920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 19
    • 0033582599 scopus 로고    scopus 로고
    • Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23 S rRNA and the synergism of their inhibitory mechanisms
    • Porse, B.T., and Garrett, R.A. (1999) Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23 S rRNA and the synergism of their inhibitory mechanisms. J Mol Biol 286: 375-387.
    • (1999) J Mol Biol , vol.286 , pp. 375-387
    • Porse, B.T.1    Garrett, R.A.2
  • 20
    • 0030573006 scopus 로고    scopus 로고
    • The donor substrate site within the peptidyl transferase loop of 23 S rRNA and its putative interactions with the CCA-end of N-blocked aminoacyl-tRNA (Phe)
    • Porse, B.T., Thi-Ngoc, H.P., and Garrett, R.A. (1996) The donor substrate site within the peptidyl transferase loop of 23 S rRNA and its putative interactions with the CCA-end of N-blocked aminoacyl-tRNA (Phe). J Mol Biol 264: 472-483.
    • (1996) J Mol Biol , vol.264 , pp. 472-483
    • Porse, B.T.1    Thi-Ngoc, H.P.2    Garrett, R.A.3
  • 21
    • 0002143814 scopus 로고    scopus 로고
    • Antibiotics and the peptidyltransferase center
    • Garrett, R.A., Douthwaite, S.R., Liljas, A, Matheson, A., Moore P.B., and Noller, H.F. (eds). Washington, DC: American Society for Microbiology Press
    • Porse, B.T., Kirillov, S.V., and Garrett, R.A. (2000) Antibiotics and the peptidyltransferase center. In The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions. Garrett, R.A., Douthwaite, S.R., Liljas, A, Matheson, A., Moore P.B., and Noller, H.F. (eds). Washington, DC: American Society for Microbiology Press, pp. 441-449.
    • (2000) The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions , pp. 441-449
    • Porse, B.T.1    Kirillov, S.V.2    Garrett, R.A.3
  • 22
    • 0034406527 scopus 로고    scopus 로고
    • Inhibition of the ribosomal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin
    • Poulsen, S.M., Kofoed, C., and Vester, B. (2000) Inhibition of the ribosomal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin. J Mol Biol 304: 471-481.
    • (2000) J Mol Biol , vol.304 , pp. 471-481
    • Poulsen, S.M.1    Kofoed, C.2    Vester, B.3
  • 23
    • 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., and 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
  • 25
    • 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 23S rRNA
    • Steiner, G., Kuechler, E., and 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 23S rRNA. EMBO J 7: 3949-3955.
    • (1988) EMBO J , vol.7 , pp. 3949-3955
    • Steiner, G.1    Kuechler, E.2    Barta, A.3
  • 26
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern, S., Moazed, D., and Noller, H.F. (1988) Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol 164: 481-489.
    • (1988) Methods Enzymol , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 27
    • 0035160878 scopus 로고    scopus 로고
    • Resistance to macrolide antibiotics conferred by base substitutions in 23S ribosomal RNA
    • Vester, B., and Douthwaite, S. (2001) Resistance to macrolide antibiotics conferred by base substitutions in 23S ribosomal RNA. Antimicrob Agents Chemother 45: 1-12.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1-12
    • Vester, B.1    Douthwaite, S.2
  • 28
    • 0028957112 scopus 로고
    • An inhibitor of ribosomal peptidyl transferase using transition-state analogy
    • Welch, M., Chastang, J., and Yarus, M. (1995) An inhibitor of ribosomal peptidyl transferase using transition-state analogy. Biochemistry 34: 385-390.
    • (1995) Biochemistry , vol.34 , pp. 385-390
    • Welch, M.1    Chastang, J.2    Yarus, M.3
  • 29
    • 0024291322 scopus 로고
    • Photochemical cross-linking of yeast tRNA (Phe) containing 8-azidoadenosine at positions 73 and 76 to the Escherichia coli ribosome
    • Wower, J., Hixson, S.S., and Zimmermann, R.A. (1988) Photochemical cross-linking of yeast tRNA (Phe) containing 8-azidoadenosine at positions 73 and 76 to the Escherichia coli ribosome. Biochemistry 27: 8114-8121.
    • (1988) Biochemistry , vol.27 , pp. 8114-8121
    • Wower, J.1    Hixson, S.S.2    Zimmermann, R.A.3
  • 30
    • 0034535129 scopus 로고    scopus 로고
    • Transit of tRNA through the Escherichia coli ribosome: Cross-linking of the 3′ end of tRNA to specific nucleotides of the 23S ribosomal RNA at the A, P and E sites
    • Wower, J., Kirillov, S.V., Wower, I.K., Guven, S.A., Hixson, S.S., and Zimmermann, R.A. (2000) Transit of tRNA through the Escherichia coli ribosome: cross-linking of the 3′ end of tRNA to specific nucleotides of the 23S ribosomal RNA at the A, P and E sites. J Biol Chem 275: 37887-37894.
    • (2000) J Biol Chem , vol.275 , pp. 37887-37894
    • Wower, J.1    Kirillov, S.V.2    Wower, I.K.3    Guven, S.A.4    Hixson, S.S.5    Zimmermann, R.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.