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PMID: 724497 Published · ppublish English Journal Article

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

Nucleic acids research ·Vol. 5 ·No. 10 ·1978-10-00 ·Pages 3643-63

Burton DR, Butler MJ, Hyde JE, Phillips D, Skidmore CJ, Walker IO

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.

MeSH Terms
Animals Cattle Cell-Free System Chromatin/ultrastructure Circular Dichroism DNA/metabolism Dose-Response Relationship, Drug Histones/metabolism Micrococcal Nuclease/metabolism Protein Binding/drug effects Sodium Chloride/pharmacology Thymus Gland
Chemicals
Chromatin Histones Sodium Chloride DNA Micrococcal Nuclease
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Burton D R
Butler M J
Hyde J E
Phillips D
Skidmore C J
Walker I O
References (18)
18 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1978-10-00
Pages
3643-63
Language
English
Region
England
NLM ID
0411011
PMCID
PMC342701
Subset
IM
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