Sequence specificity of trinucleoside diphosphate binding to polymerized tobacco mosaic virus protein.
The binding of trinucleoside diphosphates to long helical rods of tobacco mosaic virus (TMV) protein is shown to depend on base sequence, 5' AAG 3' binding being the strongest of the 25 trinucleoside diphosphate sequences measured. As TMV has a stoichiometry of three nucleotides per protein subunit, the sequence of TMV RNA suggested to be the nucleation site for self-assembly of the virus has three possible binding frames. From our binding constant data the most likely frame is predicted and shown to have two contiguous AAG sequences in a hairpin loop region.
D001483:Base Sequence; D009024:Morphogenesis; D009841:Oligonucleotides / Q000378:metabolism*; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014027:Tobacco Mosaic Virus / Q000648:ultrastructure*; D014764:Viral Proteins / Q000378:metabolism*; D014779:Virus Replication
D009841:Oligonucleotides; D014764:Viral Proteins