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Abstract
Objective. Study the influence of potato virus X envelope protein on the possibility of regulating mRNA translation in an in vitro system. Methods. Virological (virus isolation), molecular-biological (isolation of protein, mRNA and mRNP), immunochemical (serological testing), physicochemical (spectral characteristics), radiological. Results. Cytoplasmic polysomal mRNPs and membrane-bound mRNPs from Datura stramonium plants affected by potato virus X differ in spectral characteristics, as well as in composition and protein content. Polysomal mRNPs contains a protein with a molecular weight of 29 kD, which is serologically related to PVX envelope protein. When Datura stramonium is infected by the virus, PVX envelope protein tightly binds to polysomal mRNP. The remaining mRNA-bound proteins are assigned the role of protective, stabilizing, enzymatic and regulatory functions. When polysomal and membrane-bound mRNPs that we have isolated are introduced into the in vitro translation system, they direct the synthesis of a protein with a molecular weight of 29 kD, which corresponds to the mass of PVX envelope protein. The phosphorylated PVX envelope protein, introduced into the protein synthesis system in concentrations from 5 μg/mL to 25 μg/mL, using the virus-specific RNA of cytoplasmic polysomes as a matrix, plays an important role in the regulation of translation. Conclusion. Polysomal mRNPs and membrane-bound mRNPs isolated from infected thornapple plants in an in vitro protein-synthesizing system direct the synthesis of a protein with a molecular weight of 29 kD, which corresponds to the structural protein of PVX envelope. The phosphorylated potato virus X envelope protein at a concentration of 25 μg/mL suspends the synthesis of the viral protein in the in vitro translation system, which was directed by the virus-specific mRNA of cytoplasmic polysomes.
Published Version
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