Zheshovska-Vol'ny I, Sadzinska L, Grobner S, Shliankevich M A, Drize O B
Biokhimiia. 1981 Oct;46(10):1880-6.
The T-antigen of SV40 virus can be found in purified chromatin prepared from virus-induced tumour cells of the Syrian hamster. After treatment of chromatin or isolated nuclei with micrococcal nuclease this protein is detected in the high molecular weight and oligonucleosomal fractions. Data from sedimentation analysis and gel electrophoresis suggest that the T-antigen is predominantly linked with the oligonucleosomal fraction and in a lesser degree with mononucleasomes containing linker DNA and histone H1. A small amount of the T-antigen is found in the mononucleosome complex devoid of histone H1; however, the ratio of the T-antigen to DNA in this case is about 30 times less than that in the oligonucleosomal fraction. In order to investigate the nature of T-antigen binding to nucleosomes, the interaction between the T-antigen and nucleosomes from normal rat liver was studied under restricted binding of the antigen to DNA (pH 8.0). The T-antigen was effectively bound to the nucleosomes and coprecipitated with them in 5 mM MgCl2. It was shown that the T-antigen was adsorbed on columns packed with immobilized histones H1 and nucleosomal histones without H1; the former eluted at 0.15 - 0.25 M NaCl, the latter - at 0.35 - 0.5 M NaCl. The possibility of T-antigen interaction with cellular DNA and protein components of chromatin (primarily to H1) is discussed.