Abstract
The interaction of different preparations of chromatin non-histone proteins of rat liver and thymus with homologous and heterologous DNA was studied. It is shown by the method of fixation of non-histone proteins—DNA complexes on nitrocellulose filters that: (1) all the non-histone proteins preparations studied form complexes with DNA in 0.02 M Tris—HCl (pH 7.5)—3 mM MgCl 2; (2) the main part of non-histone proteins interacting with DNA binds to it non-specifically; (3) a small part of non-histone proteins interacts specifically with the homologous native DNA in 5 M urea; (4) both homologous and heterologous denatured DNA binds non-histone proteins more effectively than the native one; (5) the specific interaction of non-histone proteins with the homologous denatured DNA is observed both without urea and in its presence. The specific interaction of a small part of non-histone proteins with the homologous native and denatured DNA is also shown by the method of non-histone proteins chromatography on polyacrylamide-agarose columns containing DNA. The data obtained are discussed in the light of the possible non-histone proteins role in the specific regulation of the transcription process.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
