作者: David Zimmern
DOI: 10.1002/J.1460-2075.1983.TB01677.X
关键词: RNA 、 Nucleic acid secondary structure 、 Tobacco mosaic virus 、 Gene 、 Genetics 、 Protein secondary structure 、 Nucleic acid 、 Biology 、 Mutant 、 Nuclease 、 Biophysics
摘要: Abstract Recognition of the unique internal assembly origin on tobacco mosaic virus (TMV) RNA by disk aggregate viral coat protein probably involves an extended region (larger than that coated a single disk) folded into specific conformation. A secondary structure model is proposed for preferentially limiting amounts disks basis partial nuclease digestion data. Part this sequence can form three symmetrically spaced hairpins with marginally stable base paired sequences at tips stems. The pattern progressive protection from attack during suggests these are successively first to add. spacing identical in pseudo (part gene homologous origin). In Ni 2519, TMV mutant whose defective high temperature because it no longer discriminate between true and origins, point mutation has occurred near tip third metastably stem which would disrupt its alter one copy repeated heptanucleotide. This important role ordered cooperative recognition successive loops determining specificity assembly.