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. 1978 Oct;5(10):3643–3663. doi: 10.1093/nar/5.10.3643

The interaction of core histones with DNA: equilibrium binding studies.

D R Burton, M J Butler, J E Hyde, D Phillips, C J Skidmore, I O Walker
PMCID: PMC342701  PMID: 724497

Abstract

The binding of core histone proteins to DNA, measured as a function of [NaCl[ is a reversible process. Dissociation and reassociation occurs in two stages. Between 0.7 and 1.2 M NaCl H2a H2b bind non-cooperatively as an equimolar complex with deltaGo = 1.6 Kcals/mole at 4 degree C and 1.0 M NaCl. Between 1.2 and 2.0 M NaCl H3 and H4 bind cooperatively as an equimolar complex with delta Go = 7.4 Kcal/mole at 4 degree C and 1.0 M NaCl. The proper binding of H2a and H2b requires the presence of bound H3 and H4. Nuclease digestion of the H3-H4 DNA produces a tetramer of H3-H4 bound to fragments of DNA 145, 125 and 104 base pairs long. Thus an H3-H4 tetramer can protect fragments of DNA as long as those found in complete core particles and must therefore span the nucleosome core particle.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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