Tobacco Mosaic Virus Protein Aggregation and the Virus Assembly

Abstract

Publisher Summary This chapter describes the structure, functional design of the tobacco mosaic virus (TMV), protein aggregation, nucleation of assembly, rod elongation, selectivity for viral RNA, and general considerations. TMV is a very infectious high-yielding virus, whose properties have been highly optimized by evolution. It may therefore be possible to discern biological advantages in many of the features of its protein and RNA. Outside the plant host cell, the coat protein must ensure that the virion remains stable. Inside a susceptible plant cell, the RNA must interact with the host's biochemical machinery to ensure its own transcription and replication. TMV protein can form helical rods that are essentially the same as the protein part of the virus. Parts of TMV RNA sequence are being investigated, and sequences are available for the 71 nucleotides at the 3’-hydroxyl end and for several other oligonucleotides from within the RNA. Comparisons between these and the stronger binding regions, together with the electron density maps, may make it possible to understand the protein-nucleic acid interaction. While, it is not yet clear how generally untranslated mRNA occurs in eukaryote cells, possibly as a mechanism to allow a rapid switching one of the synthesis of specific proteins, TMV RNA may find a new experimental use in investigation of the mechanisms and control of eukaryotic protein synthesis.