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. 1974 Dec;1(12):1753–1762. doi: 10.1093/nar/1.12.1753

A new simpler photoaffinity analogue of peptidyl tRNA

Nancy Hsiung 1,2, Charles R Cantor 1,2
PMCID: PMC343454  PMID: 4616224

Abstract

The synthesis of the n-hydroxysuccinimide ester of N-(2-nitro-4-azidophenyl)glycine (NAG) is described. This reacts with E. coli phe-tRNAPhe to yield the photoaffinity label NAG-Phe-tRNAPhe. This peptidyl tRNA analogue binds correctly to the peptidyl site of the E. coli ribosome. The only significant covalent products found after irradiation of a peptidyl site bound NAG-Phe-tRNAPhe-70S-poly(U) complex are 50S proteins L11 and L18. After irradiation the complex can still bind [3H]Phe-tRNA to the amino acyl site and participate in peptide bond formation with the covalently attached NAG-Phe moiety. Alternatively, one can allow peptide bond formation to occur first, prior to photolysis. The reaction products are still L11 and L18. Hence, both of these two proteins appear to be centrally located at the peptidyl transferase center.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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