Salt-dependent interconversion of inner histone oligomers

The inner histone complex, extracted from chicken erythrocyte chromatin in 2 M NaCl at pH 7.4, has been characterized by sedimentation equilibrium and sedimentation velocity. High speed sedimentation equilibrium studies indicate that in 2 M NaCl the inner histones are a weakly associating system wit...

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Bibliographic Details
Published in:Nucleic acids research 1979-04, Vol.6 (4), p.1509-1520
Main Authors: Butler, A.P, Harrington, R.E, Olins, D.E
Format: Article
Language:English
Subjects:
animal science
Animals
Cell Nucleus - analysis
Chickens
Chromatin - ultrastructure
Erythrocytes - analysis
Histones - blood
livestock
Macromolecular Substances
Molecular Weight
Osmolar Concentration
zoology
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Summary:The inner histone complex, extracted from chicken erythrocyte chromatin in 2 M NaCl at pH 7.4, has been characterized by sedimentation equilibrium and sedimentation velocity. High speed sedimentation equilibrium studies indicate that in 2 M NaCl the inner histones are a weakly associating system with contributions from species ranging in molecular weight from dimer to octamer. The appearance of a single boundary (3.8S at 2 M NaCl) in sedimentation velocity studies conducted over a wide range of protein concentrations and ionic conditions indicates that the various histone oligomers present are in rapid equilibrium with one another. At higher salts the equilibrium is shifted to favor higher molecular weight species; in 4 M NaCl essentially all of the histone is octameric at protein concentrations above 0.2 mg/ml. The facile interconversion of histone oligomers suggests that small alterations in histone-histone interactions may be responsible for changes in nucleosome conformations during various biological processes.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/6.4.1509