Salt‐stable association of simian virus 40 capsid with simian virus 40 DNA

FEBS Letters

Bina, Minou¹  Blasquez, Veronica¹ 

[1] Chemistry Department, Purdue University, West Lafayette, IN 47907, USA

关键词: SV40 assembly;    Protein-DNA interaction;    Nucleoprotein complex;    SV40 assembly mutant;    SV40 VP1;    Nonhistone protein;   

DOI  :  10.1016/0014-5793(85)81114-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown