The nature of interactions responsible for the differences in the affinities of histones for DNA

The nature of interactions responsible for the differences in the affinities of histones for DNA

Electrophoretic studies on the sequential binding of histones to DNA and to polyphosphate in low ionic strength solution have shown that the affinities of histones for both the polyanions decreases in the same order: H4 ∼ H3 > H2A > H2B>H1. This permits to suggest that hydrophobic DNA-histo...

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Veröffentlicht in:Biochemical and biophysical research communications 1978-05, Vol.82 (2), p.674-679
Hauptverfasser: Paponov, V.D., Gromov, P.S., Sokolov, N.A., Spitkovsky, D.M., Tseitlin, P.I.
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Cattle
Chemical Phenomena
Chemistry, Physical
DNA - metabolism
Histones - metabolism
Ions
Osmolar Concentration
Polyphosphates - metabolism
Salts
Structure-Activity Relationship
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Zusammenfassung:Electrophoretic studies on the sequential binding of histones to DNA and to polyphosphate in low ionic strength solution have shown that the affinities of histones for both the polyanions decreases in the same order: H4 ∼ H3 > H2A > H2B>H1. This permits to suggest that hydrophobic DNA-histone interactions do not determine the relative affinity of histones for DNA. Non-ionic interactions within and between histone molecules participate in determining the histone affinity for DNA affecting electrostatic DNA-histone interactions.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(78)90927-0