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Salt‐stable association of simian virus 40 capsid with simian virus 40 DNA
Author(s) -
Blasquez Veronica,
Bina Minou
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81114-5
Subject(s) - nucleoprotein , capsid , simian , dna , histone , virus , population , biology , divalent , electron microscope , biophysics , microbiology and biotechnology , chemistry , virology , crystallography , biochemistry , physics , demography , organic chemistry , sociology , optics
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 apear in the electron microscope as a protein shell attached to supercoiled DNA. Consistent with this result, we find that in l M NaCl, the wildtype 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.