Tobacco rattle virus RNA-protein interactions.
For the purpose of attempting to generalize the rules concerning morphogenesis of helical viruses, the in vitro reconstitution of the CAM strain of TRV was studied. The conditions for reconstitution and the importance of the aggregation state of the protein for initiation and elongation are compared with those of TMV. The initiation step consisting of the binding of RNA with the 36S disk of protein was easily accomplished. The polarity and the specificity of encapsidation of TRV RNA by homologous and heterologous viral protein is discussed.
D066298:In Vitro Techniques; D010942:Plant Viruses / Q000378:metabolism* / Q000648:ultrastructure; D012328:RNA Viruses / Q000378:metabolism* / Q000648:ultrastructure; D012367:RNA, Viral / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D012367:RNA, Viral; D014764:Viral Proteins