Biopolym. Cell. 1989; 5(4):62-66.
Structure and Function of Biopolymers
Deoxyriboanalog of the anticodon arm of yeast tRNAPhe is not able to codon-dependent binding to small ribosomal subunits of E. coli and the rabbit liver
1Soldatkin K. A., 1Kovalchuk O. V., 1Potapov A. P., 1Elskaya A. V., 1Krynetskaya N. F., 1Dolinnaya N. G., 1Shabarova Z. A.
  1. Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR


Oligonucleotide d(CCAGACTGAAGATCTGG) has been used to study influence of sugar-phosphate backbone modifications on the interaction of tRNA anticodon region with ribosomes. Its sequence corresponds to nonmodified tRNAPheyeast anticodon arm. The oligonucleotide is shown to form an intramolecular «loop», but nevertheless it is not able to be bound to 305 and 40S ribosomes of E. coli and rabbit liver in the presence of ribo-(poly(U)) or deoxyribo-(poly(dT)) messenger. The addition of neomycin B promotes no changes in the situation.


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