Open AccessBinding of misacylated tRNAs to the ribosomal A site
Author(s) -
Taraka Dale,
Olke C. Uhlenbeck
Publication year - 2005
Publication title -
rna
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.037
H-Index - 171
eISSN - 1469-9001
pISSN - 1355-8382
DOI - 10.1261/rna.2130505
Subject(s) - transfer rna , biology , ribosome , amino acid , valine , biochemistry , ribosomal rna , aminoacyl trna , p site , translation (biology) , a site , rna , binding site , messenger rna , gene
To test whether the ribosome displays specificity for the esterified amino acid and the tRNA body of an aminoacyl-tRNA (aa-tRNA), the stabilities of 4 correctly acylated and 12 misacylated tRNAs in the ribosomal A site were determined. By introducing the GAC (valine) anticodon into each tRNA, a constant anticodon·codon interaction was maintained, thus removing concern that different anticodon·codon strengths might affect the binding of the different aa-tRNAs to the A site. Surprisingly, all 16 aa-tRNAs displayed similar dissociation rate constants from the A site. These results suggest that either the ribosome is not specific for different amino acids and tRNA bodies when intact aa-tRNAs are used or the specificity for the amino acid side chain and tRNA body is masked by a conformational change upon aa-tRNA release.
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