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Nucleic Acids Research, 1977, Vol. 4, No. 7 2293-2306
© 1977

Articles

Effect of non-histone proteins on thermal transition of chromatin and of DNA

N. Defer{dagger}, A. Kitzis{dagger}, J. Kruh{dagger}, S. Brahms* and J. Brahms*

{dagger}Institut de Pathologie Moléculaire 24 rue du Faubourg St-Jacques, 75014 Paris *Institut de Recherche en Biologie Moléculaire CNRS, Faculté des Sciences Paris VII 2 Place Jussieu, 75005 Paris, France

Received April 26, 1977. The effect of chromatin non-histone protein on DNA and chromatin stability is investigated by differential thermal denaturation method. 1) Chromtin (rat liver) yields a miltiphasic melting profile. The major part of the melting curve of this chromatin is situated at temperatures higher than pure DNA, with a distinct contribution due to nucleosomes melting. A minor part melts at temperatures lower than DNA which may be assigned to chromatin non-histone protein-DNA complex which destabilized DNA structure. 2) Heparin which extracts histones lowers the melting profile of chromatin and one observes also a contribution with a Tm lower that of pure DNA. In contrast, extraction on non-histone proteins by urea supresses the low Tm peak. 3) Reconstitution of chromatin non-histone protein-DNA complexes confirms the existence of a fraction of chromatin non-histone protein which lowers the melting temperature when compared to pure DNA. It is concluded that chromatin non-histone proteins contain different fractions of proteins which are causing stabilizing and destabilizing effects on DNA structure.


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