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Updated: Jul 6, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 26, 2011
Amino acid backbone specificity of the Escherichia coli translation machinery
Zhongping Tan1, Anthony C Forster, Stephen C Blacklow
1Department of Chemistry, Columbia University, 3000 Broadway, New York, NY 10027, USA.
Abstract:
Using a pure Escherichia coli translation system, we tested the intrinsic specificity of the protein biosynthetic machinery by determining the relative yields of peptide synthesis for incorporation of a series of acyl-%@mt;sys@%tRNA%@sx@%GAC%@be@%AsnB%@sxx@%%@mx@% 's with varied backbone structures at the sense codon GUU (Val). The results showed that different amino acids on the same tRNA adaptor give significantly different peptide yields and the potential for cross-talk between the amino acid and tRNA body/anticodon in aa-tRNA decoding by the ribosome. They further support the substrate plasticity of the ribosomal biosynthetic machinery and provide immediate candidates for ribosomally encoded polymer synthesis.
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