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Stable DNA-protein complexes in eukaryotic chromatin.

Z Avramova¹, R Tsanev

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

Journal of Molecular Biology

|July 20, 1987

Summary

Researchers identified a stable DNA-protein complex in mammalian chromatin. This complex, involving a phosphoester bond between DNA and a hydroxyamino acid, showed conserved protein components across different cell types.

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Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Mammalian chromatin structure involves complex interactions between DNA and proteins.
Understanding DNA-protein linkages is crucial for comprehending genome organization and function.

Purpose of the Study:

To investigate the nature of a persistent DNA-protein complex isolated from mammalian chromatin.
To characterize the chemical linkage and protein components of this stable complex.

Main Methods:

Isolation of DNA-protein complexes from demembranized sperm and somatic cell nuclei using high salt, urea, and detergent treatments.
Purification via CsCl density gradients.
Enzymatic digestion with DNase I and Pronase E.
Chemical analysis and two-dimensional tryptic peptide mapping.

Main Results:

A stable DNA-protein complex was isolated, resistant to extensive extraction and purification.
Digestion yielded an oligodeoxynucleotide-peptide complex, indicating a phosphoester bond between DNA and a hydroxyamino acid.
Two-dimensional peptide mapping revealed conserved protein components covalently linked to DNA across different mammalian cell types.
These protein components were distinct from mammalian topoisomerases I and II.

Conclusions:

Mammalian chromatin contains a specific DNA-protein complex with a conserved hydroxyamino acid linkage.
The identified protein component is not topoisomerase I or II, suggesting a novel DNA-binding protein.
This finding provides insights into DNA-protein interactions and chromatin stability.

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