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PMID: 940769 Published · ppublish English Journal Article

Histone dimers: a fundamental unit in histone assembly.

Nucleic acids research ·Vol. 3 ·No. 5 ·1976-05-00 ·Pages 1263-75

Sperling R, Bustin M

Abstract

Histone interactions which occur, at moderate ionic strengths, when several types of purified, renatured histones are mixed at equimolar ratios have been studied. The four histones H2A,H2B,H3 and H4 complex and form dimers. Histone H1 does not interact with the other four histone types and does not form dimers. Mixing of single histone species with preformed histone pairs as well as mixing of two different types of histone pairs, leads to exchange of histones among the pairs and formation of dimers. No trimers are formed. The dimers are in equilibrium with high-molecular weight histone structures. The results indicate that histone dimers may serve as a stable intermediate in histone assembly. Because each histone type (except H1) can interact with itself as well as with each of the other three histone types we suggest that each histone type should be considered as an interchangeable subunit of a multichain protein in which the dimer species is the most stable structure.

MeSH Terms
Animals Binding Sites Cattle Histones Macromolecular Substances Osmolar Concentration Protein Binding Protein Conformation Thymus Gland X-Ray Diffraction
Chemicals
Histones Macromolecular Substances
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sperling R
Bustin M
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26 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/3.5.1263
Published
1976-05-00
Pages
1263-75
Language
English
Region
England
NLM ID
0411011
PMCID
PMC342985
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/3.5.1263 PMC Full Text View journal details
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