Biopolym. Cell. 1988; 4(4):193-196.
Structure and Function of Biopolymers
Study of Poly(U) and poly(dT)-dependent Phe-tRNAPhe binding to 30S subunits of Escherichia coli ribosomes
- Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
Kiev, USSR
Abstract
To study the role of the codon sugar-phosphate backbones in the mRNA decoding process we have compared the messenger activity of authentic ribo- and deoxyribopolynucle-otides, poly(U) and poly(dT), in the factor-free binding of Phe-tRNAPhe to the SOS subunits of E. coli ribosomes. The template efficiency of poly(U) is much higher than that of poly(dT). Template 2'-hydroxyl groups seem to be important for the binding process at the A site of SOS subunit. The results obtained indicate the co-operative nature of the occupation of the P and A sites of SOS subunits. Neomycin exerted an insignificant effect upon the Phe-tRNAPhe binding. High sensitivity of translation efficiency to neomycin may be due to the translocation stage.
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