Identification of a coat protein binding site on southern bean mosaic virus RNA.
The cowpea strain of Southern bean mosaic virus (SBMV-C), a T = 3 icosahedral RNA virus, was dissociated to yield a ribonucleoprotein complex (RNPC) composed of the viral RNA and coat protein subunits. To determine if the coat protein subunits were bound to a specific site on the viral RNA, the RNPC was treated with ribonuclease, and the remaining coat protein--RNA complexes were recovered by filter binding. A single species of RNA was isolated by this procedure and further characterized by sequencing. The RNA was mapped to nucleotides 1410-1436 of the SBMV-C genome. This region of the viral RNA was predicted to fold into a hairpin with a 4-base loop and a duplex stem of 24 nucleotides. The stability and specificity of the coat protein-RNA complex isolated from dissociated virus suggest a possible role for this interaction in the selective encapsidation of the viral RNA.
Hacker
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Department of Microbiology, University of Tennessee, Knoxville 37996-0845.
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D002213:Capsid / Q000378:metabolism*; D002874:Chromosome Mapping; D017798:Comovirus / Q000235:genetics* / Q000378:metabolism*; D007887:Fabaceae / Q000821:virology; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D016366:Open Reading Frames; D010946:Plants, Medicinal; D011485:Protein Binding; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D012367:RNA, Viral