共 58 条
Uniform binding of aminoacylated transfer RNAs to the ribosomal A and P sites
被引:86
作者:

Fahlman, RP
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Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA

Dale, T
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机构:
Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA

Uhlenbeck, OC
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机构:
Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA
机构:
[1] Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA
关键词:
D O I:
10.1016/j.molcel.2004.10.030
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The association and dissociation rate constants of eight different E. coli aminoacyl-tRNAs (aa-tRNAs) for E. coli ribosomes programmed with mRNAs of defined sequences were determined. Identical association and dissociation rate constants were observed for all eight aa-tRNAs in both the ribosomal A and P sites despite substantial differences in tRNA sequence, the type of esterified amino acid, and posttranscriptional modifications. These results indicate that the overall binding of all aa-tRNAs to the ribosome is uniform. However, when either the esterified amino acid or the tRNA modifications were removed, binding was no longer uniform. These results suggest that differences in tRNA sequences and tRNA modifications have evolved to offset differential thermodynamic contributions of the esterified amino acid and the codon-anticodon interaction so that ribosomal binding of all aa-tRNAs remains uniform.
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页码:799 / 805
页数:7
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