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  Codon-Anticodon Interaction at the P Site Is a Prerequisite for tRNA Interaction with the Small Ribosomal Subunit

Schäfer, M. A., Tastan, A. Ö., Patzke, S., Blaha, G., Spahn, C. M. T., Wilson, D. N., et al. (2002). Codon-Anticodon Interaction at the P Site Is a Prerequisite for tRNA Interaction with the Small Ribosomal Subunit. Journal of Biological Chemistry, 277(21), 19095-19105.

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Schäfer, Markus A.1, Autor
Tastan, A. Özlem1, Autor
Patzke, Sebastian1, Autor
Blaha, Gregor2, Autor           
Spahn, Christian M. T.3, Autor           
Wilson, Daniel N.3, Autor           
Nierhaus, Knud H.2, Autor           
Affiliations:
1Max Planck Society, ou_persistent13              
2Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              
3Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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 Zusammenfassung: The arrival of high resolution crystal structures for the ribosomal subunits opens a new phase of molecular analysis and asks for corresponding analyses of ribosomal function. Here we apply the phosphorothioate technique to dissect tRNA interactions with the ribosome. We demonstrate that a tRNA bound to the P site of non-programmed 70 S ribosomes contacts predominantly the 50 S, as opposed to the 30 S subunit, indicating that codon-anticodon interaction at the P site is a prerequisite for 30 S binding. Protection patterns of tRNAs bound to isolated subunits and programmed 70 S ribosomes were compared. The results suggest the presence of a movable domain in the large ribosomal subunit that carries tRNA and reveal that only ~15% of a tRNA, namely residues 30 ± 1 to 43 ± 1, contact the 30 S subunit of programmed 70 S ribosomes, whereas the remaining 85% make contact with the 50 S subunit. Identical protection patterns of two distinct elongator tRNAs at the P site were identified as tRNA species-independent phosphate backbone contacts. The sites of protection correlate nicely with the predicted ribosomal-tRNA contacts deduced from a 5.5-Å crystal structure of a programmed 70 S ribosome, thus refining which ribosomal components are critical for tRNA fixation at the P site.

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Sprache(n): eng - English
 Datum: 2002-02-26
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
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 Identifikatoren: eDoc: 24483
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Titel: Journal of Biological Chemistry
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 277 (21) Artikelnummer: - Start- / Endseite: 19095 - 19105 Identifikator: -