The ribosome is a dynamic machine that undergoes dramatic conformational changes during the elongation cycle of protein biosynthesis. In order to be useful in ribosomal function, there are specific regions in rRNA which are highly conserved, single stranded and exposed on the ribosomal surface. We selected in plant material (Lupinus luteus) seven of them to be investigated with the antisense strategy as a research tool. Small complementary, radiolabeled oligodeoxymers were used to hybridize to specific regions in 18S rRNA in the ribosomes converted to four different conformational stages. The effects of probe hybridization on the model polypeptide biosynthesis were measured using a nitrocellulose filtration binding assay. Site specificity of the oligomer binding was assured using bioinformatics algorithms, thermodynamic analysis and saturation assays. We found inhibition of the aminoacyl-tRNA binding (up to 84%) due to specific hybridization of the oligomers addressed to the selected fragments of 18S rRNA. We present the evidence for the key role played by these regions of rRNAs during protein biosynthesis in plant system. We observed well defined structural changes of ribosome’s conformation during different steps of the elongation cycle of protein biosynthesis.

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