It is shown that the concentration of "antisignature" phosphorothioate analogs of oligodeoxynucleotides, complementary to the region of 165 rRNA Acholeplasma laidlawii PG-8 and Mycoplasma fermentans PG-18 responsible tor binding with ribosomal protein S4 being 0.5--1 microM synthesis of proteins in vivo decreases to 70%. A model of mechanisms is suggested to block oligonucleotides of the process of in vivo translation in mollicutes by "antisignature" phosphorothioate analogs. The advantages of the use of antisense oligonucleotides complementary to functionally significant plots of 16S rRNA to inhibit the in vivo translation are discussed in comparison with oligonucleotides, 5-nontranslated regions of mRNA serving a target for them.
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Processes of absorption and uptake of phosphorothioate, phosphorodithioate and methylphosphonate analogs of oligodeoxynucleotides which are complementary to "signature" 16S rRNA sequences by cells of Acholeplasma laidlawii PG-8. Mycoplasma fermentans PG-18 and Mycoplasma pneumoniae FH have been investigated. Distinctions in efficiency of absorption by given cells of phosphorothioate and methylphosphonate analogs of oligonucleotides are found out.
View Article and Find Full Text PDFIt is shown that the concentration of "antisignature" phosphorothioate analogs of oligodeoxynucleotides, complementary to the region of 165 rRNA Acholeplasma laidlawii PG-8 and Mycoplasma fermentans PG-18 responsible tor binding with ribosomal protein S4 being 0.5--1 microM synthesis of proteins in vivo decreases to 70%. A model of mechanisms is suggested to block oligonucleotides of the process of in vivo translation in mollicutes by "antisignature" phosphorothioate analogs.
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