title: Salt-stable association of simian virus 40 capsid with simian virus 40 DNA.
abstract: In 8 M CsCl, a fraction of the wild-type previrions and tsB228 nucleoprotein complexes lose their core histones but retain their capsid. These histone-depleted complexes appear in the electron microscope as a protein shell attached to supercoiled DNA. Consistent with this result, we find that in 1 M NaCl, the wild-type previrions dissociate into two populations of nucleoprotein complexes. One population sediments between 50 and 140 S and morphologically resembles the shell-DNA complexes isolated in CsCl gradients. The other population is comprised primarily of nucleoproteins which sediment at 40 S.
authors.forename: V
authors.initials: V
authors.lastname: Blasquez
authors.forename: M
authors.initials: M
authors.lastname: Bina
mesh_terms: D002213:Capsid / Q000378:metabolism*; D002499:Centrifugation, Density Gradient; D002868:Chromosomal Proteins, Non-Histone / Q000032:analysis; D004278:DNA, Superhelical / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism*; D008854:Microscopy, Electron; D009698:Nucleoproteins / Q000032:analysis; D013539:Simian virus 40
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D004278:DNA, Superhelical; D004279:DNA, Viral; D009698:Nucleoproteins