The interaction of histones with simian virus 40 supercoiled circular deoxyribonucleic acid in vitro.
The interaction of supercoiled, circular SV40 DNA with calf thymus histone fractions has been studied. Five- to ten-fold less f1 histone is required to complex a given amount of DNA compared to the other histones. When the supercoiled DNA is converted to either the relaxed circular form, or full length linear molecules, or gragmented linear or denatured stands, the efficiency of complex formation with f1 histone markedly decreases. We conclude that f1 histone has a special ability to interact with supercoiled DNA. This conclusion is supported by the fact that supercoiled circular Col E1 DNA interacts with f1 as efficiently as does SV40 DNA.
D000818:Animals; D002417:Cattle; D004279:DNA, Viral; D006657:Histones; D046911:Macromolecular Substances; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D011485:Protein Binding; D011487:Protein Conformation; D013539:Simian virus 40 / Q000378:metabolism; D013936:Thymidine / Q000378:metabolism; D013950:Thymus Gland
D004279:DNA, Viral; D006657:Histones; D046911:Macromolecular Substances; D013936:Thymidine