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          Institute: MPI für molekulare Genetik     Collection: Ribosome Research Groups     Display Documents



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ID: 224135.0, MPI für molekulare Genetik / Ribosome Research Groups
Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: the universally conserved residues G693 and C795 regulate P-site RNA binding
Authors:Dinos, George; Wilson, Daniel N.; Teraoka, Yoshika; Szaflarski, Witold; Fucini, Paola; Kalpaxis, Dimitrios; Nierhaus, Knud H.
Language:English
Date of Publication (YYYY-MM-DD):2004-01-15
Title of Journal:Molecular Cell
Journal Abbrev.:Mol Cell
Volume:13
Issue / Number:1
Start Page:113
End Page:124
Copyright:© 2004 Cell Press
Review Status:not specified
Audience:Experts Only
Abstract / Description: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.
External Publication Status:published
Document Type:Article
Communicated by:Ribosome Group
Affiliations:MPI für molekulare Genetik
External Affiliations:Department of Biochemistry, School of Medicine, University of Patras, 26500 Patras, Greece
Identifiers:ISBN:1097-2765
DOI:10.1016/S1097-2765(04)00002-4
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