Phosphorylation of Tobacco Mosaic Virus Movement Protein Abolishes Its Translation Repressing Ability

• Published in: Virology (New York, N.Y.) N.Y.), 1999-08, Vol.261 (1), p.20-24
• Main Authors: Karpova, O.V., Rodionova, N.P., Ivanov, K.I., Kozlovsky, S.V., Dorokhov, Yu.L., Atabekov, J.G.
• Format: Article
• Language: English
• Subjects: Brassica - enzymology; Brassica - virology; Cell Wall - enzymology; Gene Expression Regulation; infection; movement protein; Nicotiana - enzymology; Nicotiana - virology; Phosphorylation; Plant Viral Movement Proteins; Plants, Toxic; Protein Biosynthesis; Protein Kinase C - metabolism; Protein Kinases - metabolism; regulation of translation; ribonucleoprotein complexes; Ribonucleoproteins - metabolism; RNA, Viral - metabolism; TMV; Tobacco mosaic virus; Tobacco Mosaic Virus - genetics; Tobacco Mosaic Virus - metabolism; Tobacco Mosaic Virus - physiology; Viral Proteins - genetics; Viral Proteins - metabolism; Viral Proteins - physiology
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1006/viro.1999.9842

Previously we showed that the ribonucleoprotein complexes (RNPs) of the TMV 30-kDa movement protein (MP) with TMV RNA are nontranslatable in vitro and noninfectious to protoplasts, but are infectious to intact plants. It has been suggested that MP–TMV RNA complexes could be converted into the translatable and replicatable form in planta in the course of passage through plasmodesmata (Karpova et al., 1997, Virology 230, 11–21). The role of TMV MP phosphorylation was investigated in terms of its capacity to modulate the translation-repressing ability of the MP. Phosphorylation of the TMV MP, either before or after RNP complex formation, caused a conversion of nontranslatable MP–RNA complexes into a form that was translatable in vitro and infectious to protoplasts and plants.