Biopolym. Cell. 1990; 6(4):59-65.
Structure and Function of Biopolymers
Studies in the interaction of the tRNAPhe derivative bearing an arylazide group on its G24 residue with Escherichia coli ribosomes and tRNA-(adenine-l-)methyl transferase from Thermus thermophilus
1Venkstern T. V., 2Graifer D. M., 2Karpova G. G., 1Morozov I. A.
  1. Engelhardt Institute of Molecular Biology, Academy of Sciences of the USSR
    Moscow, USSR
  2. Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR
    Novosibirsk, USSR

Abstract

Photoaffinity labelling of E. coli ribosomes and tRNA (adenine-1-)methyl transferase has been studied using E. coli tRNAPhe derivative bearing an aryl-azide group on its Gj4 residue. Under UV-irradiation (λ > 310 nm) this derivative is shown to be cross-linked to tRNA(adenine-l-)methyl transferase from T. thermophilus but being located at ribosomal A or P site no cross-linking of the tRNA derivative to the ribosomes is observed.

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