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  Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: the universally conserved residues G693 and C795 regulate P-site RNA binding

Dinos, G., Wilson, D. N., Teraoka, Y., Szaflarski, W., Fucini, P., Kalpaxis, D., et al. (2004). Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: the universally conserved residues G693 and C795 regulate P-site RNA binding. Molecular Cell, 13(1), 113-124. doi:10.1016/S1097-2765(04)00002-4.

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Genre: Zeitschriftenartikel
Alternativer Titel : Mol Cell

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 Urheber:
Dinos, George, Autor
Wilson, Daniel N.1, Autor           
Teraoka, Yoshika2, Autor
Szaflarski, Witold3, Autor           
Fucini, Paola3, Autor           
Kalpaxis, Dimitrios, Autor
Nierhaus, Knud H.3, Autor           
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Max Planck Society, ou_persistent13              
3Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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 Zusammenfassung: The crystal structures of the universal translation-initiation inhibitors edeine and pactamycin bound to ribosomal 30S subunit have revealed that edeine induces base pairing of G693:C795, residues that constitute the pactamycin binding site. Here, we show that base pair formation by addition of edeine inhibits tRNA binding to the P site by preventing codon-anticodon interaction and that addition of pactamycin, which rebreaks the base pair, can relieve this inhibition. In addition, edeine induces translational misreading in the A site, at levels comparable to those induced by the classic misreading antibiotic streptomycin. Binding of pactamycin between residues G693 and C795 strongly inhibits translocation with a surprising tRNA specificity but has no effect on translation initiation, suggesting that reclassification of this antibiotic is necessary. Collectively, these results suggest that the universally conserved G693:C795 residues regulate tRNA binding at the P site of the ribosome and influence translocation efficiency.

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Sprache(n): eng - English
 Datum: 2004-01-15
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: eDoc: 224135
DOI: 10.1016/S1097-2765(04)00002-4
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Titel: Molecular Cell
  Alternativer Titel : Mol Cell
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 13 (1) Artikelnummer: - Start- / Endseite: 113 - 124 Identifikator: ISBN: 1097-2765