title: Assembly of a rod-shaped virus.  Disk aggregate of cucumber green mottle mosaic virus protein and its function.
abstract: Although it is established that in the assembly of tobacco mosaic virus (TMV) in vitro, a 20 S disk aggregate of protein is essential for the initiation of the reaction, there is no agreement as to whether subsequent rod elongation proceeds by the addition of protein subunits or disks.  Cucumber green mottle mosaic virus (CGMMV) is a rod-shaped virus closely related to TMV.  It was observed directly by electron microscopy that CGMMV-protein also formed a single- or double-layer disk aggregate under conditions where reconstitution with the protein and TMV-RNA proceeds efficiently.  Whichever forms, a single or double layer, a disk aggregate is required for the initiation of reconstitution, but cannot participate in rod elongation.  These results obtained with CGMMV support our model proposed for the mechanism of assembly of TMV and rod-shaped viruses; i.e., the assembly occurs in two steps; disk aggregates of protein are essential only for initiation, and rod eleongation proceeds by subsequent addition of subunits.
mesh_terms: D004355:Drug Stability; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D009029:Mosaic Viruses / Q000648:ultrastructure*; D010942:Plant Viruses / Q000648:ultrastructure*; D011485:Protein Binding; D013045:Species Specificity; D013696:Temperature; D013997:Time Factors; D014027:Tobacco Mosaic Virus / Q000648:ultrastructure; D014461:Ultracentrifugation; D014764:Viral Proteins / Q000032:analysis; D014779:Virus Replication
chemical_list: D046911:Macromolecular Substances; D014764:Viral Proteins