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  • Title: [The type of interaction of histone H5 wo ith DNA changes significantly at various stages of chromatin condensation].
    Author: Pruss DV, Ebralidze KK, Mirzabekov AD.
    Journal: Mol Biol (Mosk); 1988; 22(4):1108-18. PubMed ID: 3185531.
    Abstract:
    Histones were covalently bound to DNA by dimethylsulfate-induced crosslinking and DNA-contacting peptides of histone H5, thus modified, were mapped by a combination of peptide cleavage reactions and peptide gel electrophoresis. In the nucleosome, the only strong crosslinking point is His-25 which resides near the ends of nucleosomal DNA. This contact point persists throughout different steps of chromatin condensation--decondensation. In decondensed chromatin, it is supplemented by the contact with DNA of the N-terminus of the histone H5 molecule. The high level of chromatin condensation existing in the nuclei or induced by bivalent cations results in a new and considerably stronger crosslinking point His-62, which is also characteristic for cooperative H5-DNA complexes. This structural change is observed only on oligonucleosomal chains containing no less than 3 contiguous nucleosomes, and is absent in isolated mono- or dinucleosomes. We propose that the formation of the 30-nm chromatin fibre, typical for the nuclei, is accomplished in part by the histone H5-linker DNA cooperative interactions, manifested by strong His-62--linker DNA contact.
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