Isolation and analysis of virus-specific ribonucleoprotein of tobacco mosaic virus-infected tobacco
1983; Elsevier BV; Volume: 127; Issue: 2 Linguagem: Inglês
10.1016/0042-6822(83)90141-1
ISSN1096-0341
AutoresYuri L. Dorokhov, N.M. Alexandrova, N.A. Miroshnichenko, J.G. Atabekov,
Tópico(s)Plant and Fungal Interactions Research
ResumoA ribonucleoprotein fraction (vRNP) of a characteristic buoyant density greater than the buoyant density of tobacco mosaic virus (TMV) particles has been isolated from infected tissue by Cs2SO4 density gradient centrifugation. The vRNP particles appear to be TMV specific because they are synthesized in the presence of actinomycin D and have RNAs identified as genomic and I-class subgenomic (apparent Mr 1.1–1.3 × 106 and 0.60.8 × 106) RNAs by their electrophoretic mobility and hybridization to plasmid-bearing RNA sequences. Polypeptides of apparent molecular weights 17,500 (TMV coat), 31,000, 37,000, and 39,000 were major constituents of vRNP. Of the minor polypeptides, those of apparent molecular weights 70,000, 68,000, 55,000, and 25,000 had electrophoretic mobilities similar to mobilities of polypeptides found in a ribonucleoprotein preparation from uninoculated plants. vRNP from common TMV-infected plants, but not from plants infected with a mutant that did not form native coat protein, reacted with immunoglobins against TMV and TMV coat protein. Common TMV and its vRNP differed in the extent of reactivity toward the two immunoglobins, in electron microscopic appearance, and in the higher sensitivity of vRNP to ribonuclease.
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