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J Mol Biol. 1987 Jul 20;196(2):437-40.

Stable DNA-protein complexes in eukaryotic chromatin.

Author information

1
Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia.

Abstract

Demembranized sperm and somatic nuclei of mammalian origin were extracted with high salt/urea/2-mercaptoethanol, treated with detergents and purified in CsCl density gradients to isolate DNA. Under these conditions a protein component still remained bound to DNA. This stable DNA-protein complex could be reduced to an oligodeoxynucleotide-peptide complex by extensive sequential digestions with DNase I and Pronase E. Chemical and enzymatic treatments of this complex indicated the presence of a phosphoester bond between DNA and a hydroxyamino acid. Two-dimensional tryptic peptide mapping revealed a remarkable similarity among the covalently linked protein components in all types of chromatin studied. These maps differed from the maps of mammalian topoisomerases I and II.

PMID:
3656455
DOI:
10.1016/0022-2836(87)90704-2
[Indexed for MEDLINE]

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