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PMID: 197520 Published · ppublish English Journal Article

Crosslinked histone octamer as a model of the nucleosome core.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 7 ·1977-07-00 ·Pages 2780-4

Stein A, Bina-Stein M, Simpson RT

Abstract

When histones in chromatin core particles were crosslinked with dimethylsuberimidate, the resulting particles had properties closely similar to those of native core particles. A crosslinked octameric histone complex was isolated from these particles under nondenaturing conditions. Upon reaction with DNA, this octameric protein folded the DNA into a structure closely resembling that of native core particles as verified by various techniques; protein denaturants were necessary for reassociation. The histone octamer is useful as a model of the nucleosome protein core and for studying histone-DNA interactions that occur in nucleosomes.

MeSH Terms
Chromatin/ultrastructure Circular Dichroism DNA/metabolism DNA, Circular/metabolism DNA, Viral/metabolism Histones/metabolism Models, Structural Nucleic Acid Conformation Nucleic Acid Denaturation Protein Binding Protein Conformation Simian virus 40 Temperature
Chemicals
Chromatin DNA, Circular DNA, Viral Histones DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Stein A
Bina-Stein M
Simpson R T
References (31)
31 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.74.7.2780
Published
1977-07-00
Pages
2780-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431287
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.7.2780 PMC Full Text View journal details
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