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Nucleic Acids Research, 1991, Vol. 19, No. 15 4199-4201
© 1991

MOLECULAR BIOLOGY

Interaction of ribo- and deoxyriboanalogs of yeast tRNAPhe anticodon arm with programmed small ribosomal subunits of Escherichia coli and rabbit liver

Oleg V. Koval'chuke, Anatoly P. Potapov, Anna V. El'skaya*, Viktor K. Potapov1, Nataliya F. Krinetskaya1, Nina G. Dolinnaya1 and Zoya A. Shabarova1

lnstitute of Molecular Biology and Genetics 150 Zabolotnogo Str, 252627 Kiev, USSR 1Moscow State University 119899, Moscow, USSR

* To whom correspondence should be addressed

Received April 5, 1991. Revised July 4, 1991. Accepted July 4, 1991.

A synthetic ribooligonucleotide, r(CCAGACUGm-AAG AUCUGG), corresponding to the unmodified yeast tRNAPhe anticodon arm is shown to bind to poly(U) programmed small ribosomal subunits of both E.coli and rabbit liver with affinity two order less than that of a natural anticodon arm. Its deoxyriboanalogs d(CCAGACTGAAGATCTGG) and d(CCAGA)r(CUGm-AAG-A)d(TCTGG), are used to study the influence of sugar-phosphate modification on the interaction of tRNA with programmed small ribosomal subunits. The deoxyribooligonucleotide is shown to adopt a hairpin structure. Nevertheless, as well as oligonucleotide with deoxyriboses in stem region, it is not able to bind to 30S or 40S ribosomal subunits in the presence of ribo(poly(U)) or deoxyribo-(poly (dT) template. The deoxyribooligonucleotide also has no inhibitory effect on tRNAPhe binding to 30S ribosomes at 10-fold excess over tRNA. Neomycin does not influence binding of tRNA anticodon arm analogs used. Complete tRNA molecule and natural modifications of anticodon arm are considered to stabilize the arm structure needed for its interaction with a programmed ribosome.


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