Rearrangement of nucleosomal components by modification of histone amino groups. Structural role of lysine residues

Modification of nucleosomal particles from chicken erythrocytes with the reagents for protein amino groups acetic and dimethylmaleic anhydrides causes a rearrangement of nucleosomal components. Treatment with both reagents is accompanied by liberation of free DNA and formation of residual particles...

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Bibliographic Details
Published in:Biochemistry (Easton) 1984-09, Vol.23 (19), p.4280-4284
Main Authors: Jordano, Juan, Montero, Francisco, Palacian, Enrique
Format: Article
Language:English
Subjects:
Animals
Centrifugation, Density Gradient
Chickens
DNA
DNA - metabolism
Electrophoresis, Polyacrylamide Gel
erythrocytes
Erythrocytes - ultrastructure
histones
Histones - analysis
lysine
Lysine - physiology
Maleic Anhydrides - pharmacology
Nucleic Acid Conformation
nucleosomes
Nucleosomes - ultrastructure
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Summary:Modification of nucleosomal particles from chicken erythrocytes with the reagents for protein amino groups acetic and dimethylmaleic anhydrides causes a rearrangement of nucleosomal components. Treatment with both reagents is accompanied by liberation of free DNA and formation of residual particles with anomalous histone composition. The residual particles obtained with acetic anhydride contain an excess of histones corresponding to the free DNA produced. In contrast, dimethylmaleic anhydride causes release of histones H1, H5, H2A and H2B and formation of residual particles deficient in these histones but containing an excess of H3 and H4 corresponding to the liberated DNA. Regeneration of the modified amino groups of nucleosomal preparations treated with dimethylmaleic anhydride is accompanied by reconstitution of nucleosomal particles with the sedimentation coefficient and composition of core histones of the original nucleosomes. This reconstitution does not occur when the released fraction containing histones H2A and H2B and free DNA is separated from the residual particles. The studied disassembly of nucleosomal particles obtained by specifically blocking lysine-DNA interactions with these reagents appears to indicate that lysine residues are essential for the binding of DNA to histones with formation of nucleosomal particles.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00314a004