The assembly of papaya mosaic virus coat protein with DNA.
Products of specific (pH 8.0-8.5) and nonspecific (pH 6.0) assembly reactions of papaya mosaic virus (PMV) coat protein with DNA are described. The strandedness, topology, and sugar moiety of the nucleic acid are important parameters for assembly in nonspecific conditions. The linear, single-stranded form of lambda DNA, but not the double-stranded form, reacted with PMV protein to form multiply initiated particles whose helical segments apparently annealed to produce continuous tubular particles. With the circular, single-stranded DNA of phi X174, partially tubular, partially extended particles were made. Poly(dA), unlike poly(A) [Erickson JW, AbouHaidar M, Bancroft JB: Virology 90:60, 1978], was not encapsidated by PMV protein under specific assembly conditions. With all DNAs tested, extended particles were the only products formed in specific conditions at pH 8.5.
D010582:Bacteriophage lambda; D001665:Binding Sites; D004270:DNA, Circular / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism*; D008854:Microscopy, Electron; D009024:Morphogenesis; D009029:Mosaic Viruses / Q000648:ultrastructure*; D011485:Protein Binding; D014764:Viral Proteins / Q000378:metabolism*
D004270:DNA, Circular; D004277:DNA, Single-Stranded; D004279:DNA, Viral; D014764:Viral Proteins